1hc6 - Revision history

OCA: Redirecting to 1hc1

2008-10-01T18:24:51Z

Redirecting to 1hc1

←Older revision		Revision as of 18:24, 1 October 2008
Line 1:		Line 1:
-	~~{{Seed}}~~	+	#REDIRECT [[1hc1]] This PDB entry is obsolete and replaced by 1hc1
-	[[~~Image:1hc6.png\|left\|200px~~]]	+
-		+
-	~~<!--~~	+
-	~~The line below this paragraph, containing "STRUCTURE_1hc6", creates the "Structure Box" on the page.~~	+
-	~~You may change the~~ PDB ~~parameter (which sets the PDB file loaded into the applet)~~	+
-	~~or the SCENE parameter (which sets the initial scene displayed when the page~~ is ~~loaded),~~	+
-	~~or leave the SCENE parameter empty for the default display.~~	+
-	~~-->~~	+
-	~~{{STRUCTURE_1hc6\| PDB=1hc6 \| SCENE= }}~~	+
-		+
-	~~===CRYSTAL STRUCTURE OF HEXAMERIC HAEMOCYANIN FROM PANULIRUS INTERRUPTUS REFINED AT 3.2 ANGSTROMS RESOLUTION===~~	+
-		+
-		+
-	~~<!--~~	+
-	~~The line below this paragraph, {{ABSTRACT_PUBMED_2585484}}, adds the Publication Abstract to the page~~	+
-	~~(as it appears on PubMed at http://www.pubmed.gov), where 2585484 is the PubMed ID number.~~	+
-	~~-->~~	+
-	~~{{ABSTRACT_PUBMED_2585484}}~~	+
-		+
-	~~==About this Structure==~~	+
-	1HC6 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Panulirus_interruptus Panulirus interruptus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HC6 OCA].	+
-		+
-	~~==Reference==~~	+
-	Crystal structure of hexameric haemocyanin from Panulirus interruptus refined at 3.2 A resolution., Volbeda A, Hol WG, J Mol Biol. 1989 Sep 20;209(2):249-79. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/2585484 2585484]	+
-	~~[[Category: Panulirus interruptus]]~~	+
-	~~[[Category: Single protein]]~~	+
-	~~[[Category: Hol, W G.J.]]~~	+
-	~~[[Category: Volbeda, A.]]~~	+
-	~~[[Category: Oxygen transport]]~~	+
-		+
-	~~''Page seeded~~ by ~~[http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 07:58:18 2008''~~	+

OCA at 04:58, 1 July 2008

2008-07-01T04:58:20Z

←Older revision		Revision as of 04:58, 1 July 2008
Line 1:		Line 1:
-	[[Image:1hc6.~~jpg~~\|left\|200px]]	+	{{Seed}}
		+	[[Image:1hc6.png\|left\|200px]]

	<!--		<!--
Line 9:		Line 10:
	{{STRUCTURE_1hc6\| PDB=1hc6 \| SCENE= }}		{{STRUCTURE_1hc6\| PDB=1hc6 \| SCENE= }}

-	~~'''~~CRYSTAL STRUCTURE OF HEXAMERIC HAEMOCYANIN FROM PANULIRUS INTERRUPTUS REFINED AT 3.2 ANGSTROMS RESOLUTION~~'''~~	+	===CRYSTAL STRUCTURE OF HEXAMERIC HAEMOCYANIN FROM PANULIRUS INTERRUPTUS REFINED AT 3.2 ANGSTROMS RESOLUTION===


-	~~==Overview==~~	+	<!--
-	~~The use of non~~-crystallographic symmetry restraints in the refinement of the haemocyanin hexamer from Panulirus interruptus at 3.2 A resolution has resulted in a final model with a very reasonable geometry and a crystallographic R-~~factor of 20.1%, using 59,193 observed structure factor amplitudes between 8.0 and 3.2 A.~~ The mean co-ordinate error is approximately 0.35 A. The six subunits appear to be related by symmetry operations that differ slightly from 32 point group symmetry. The six subunits have essentially maintained the same structure. The hexamer, ~~with point group 32~~, ~~is best described as a trimer of "tight dimers". The contacts between~~ the subunits in such a dimer are more numerous, and better conserved during evolution than contacts in a trimer. The interface of a tight dimer is separated by an internal cavity into two "contact areas". The contact area nearest to the centre of the hexamer is most extensive and consists mainly of residues that are quite conserved among arthropodan haemocyanins. All these residues are provided by the second domain of each subunit. Hence, this second domain may play a crucial role in the allosteric functioning of this oxygen transport protein. The dinuclear copper oxygen-binding site resides in the centre of domain 2. This oxygen-binding centre is not fully accessible from the solvent. Three large cavities occur, however, within each subunit at ~~the interfaces of the three domains~~. ~~All three cavities contain ordered water molecules, and two of them are accessible from the surrounding solvent~~. ~~These cavities may play a role in facilitating fast movement of dioxygen towards the binding site~~, ~~which~~ is ~~situated in a highly conserved, rather hydrophobic core. A detailed definition of~~ the ~~geometry of the copper site is, of course, not possible at the limited resolution of 3~~.~~2 A. Nevertheless, it is possible to conclude that each copper is co~~-~~ordinated by two, more or less tightly bound, histidine ligands and one more distant histidine residue. The six histidine residues utilize their N epsilon atoms for copper co~~-ordination, while their N delta atoms are engaged in hydrogen bonds with conserved residues or water molecules. The two distant histidine ligands are located in apical positions and are on opposite sides with respect to the plane approximately defined by the four more tightly bound histidine ligands and the two copper ions. The copper-to-copper distance is 3.5 to 3.6 A in four of the subunits, but this distance deviates considerably in two others.(ABSTRACT TRUNCATED AT 400 WORDS)	+	The line below this paragraph, {{ABSTRACT_PUBMED_2585484}}, adds the Publication Abstract to the page
		+	(as it appears on PubMed at http://www.pubmed.gov), where 2585484 is the PubMed ID number.
		+	-->
		+	{{ABSTRACT_PUBMED_2585484}}

	==About this Structure==		==About this Structure==
Line 25:		Line 29:
	[[Category: Volbeda, A.]]		[[Category: Volbeda, A.]]
	[[Category: Oxygen transport]]		[[Category: Oxygen transport]]
-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Fri May~~ ~~2 18~~:41:19 2008''	+
		+	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 07:58:18 2008''

OCA at 15:41, 2 May 2008

2008-05-02T15:41:19Z

←Older revision		Revision as of 15:41, 2 May 2008
Line 1:		Line 1:
	[[Image:1hc6.jpg\|left\|200px]]		[[Image:1hc6.jpg\|left\|200px]]

-	~~{{Structure~~	+	<!--
-	~~\|PDB= 1hc6 \|SIZE=350\|CAPTION= <scene name='initialview01'>1hc6</scene>~~, ~~resolution 3~~.~~2Å~~	+	The line below this paragraph, containing "STRUCTURE_1hc6", creates the "Structure Box" on the page.
-	~~\|SITE=~~	+	You may change the PDB parameter (which sets the PDB file loaded into the applet)
-	~~\|LIGAND= <~~scene ~~name='pdbligand=CU:COPPER+(II~~)~~+ION'>CU</scene>~~	+	or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
-	~~\|ACTIVITY=~~	+	or leave the SCENE parameter empty for the default display.
-	~~\|GENE=~~	+	-->
-	\|~~DOMAIN~~=	+	{{STRUCTURE_1hc6\| PDB=1hc6 \| SCENE= }}
-	\|~~RELATEDENTRY~~=	+
-	\|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1hc6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hc6 OCA], [http://www.ebi.ac.uk/pdbsum/1hc6 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1hc6 RCSB]</span>	+
-	}}	+

	'''CRYSTAL STRUCTURE OF HEXAMERIC HAEMOCYANIN FROM PANULIRUS INTERRUPTUS REFINED AT 3.2 ANGSTROMS RESOLUTION'''		'''CRYSTAL STRUCTURE OF HEXAMERIC HAEMOCYANIN FROM PANULIRUS INTERRUPTUS REFINED AT 3.2 ANGSTROMS RESOLUTION'''
Line 27:		Line 24:
	[[Category: Hol, W G.J.]]		[[Category: Hol, W G.J.]]
	[[Category: Volbeda, A.]]		[[Category: Volbeda, A.]]
-	[[Category: ~~oxygen~~ transport]]	+	[[Category: Oxygen transport]]
-		+	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 18:41:19 2008''
-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Sun Mar 30 21~~:02:06 2008''	+

OCA at 18:02, 30 March 2008

2008-03-30T18:02:08Z

←Older revision		Revision as of 18:02, 30 March 2008
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	\|PDB= 1hc6 \|SIZE=350\|CAPTION= <scene name='initialview01'>1hc6</scene>, resolution 3.2Å		\|PDB= 1hc6 \|SIZE=350\|CAPTION= <scene name='initialview01'>1hc6</scene>, resolution 3.2Å
	\|SITE=		\|SITE=
-	\|LIGAND= <scene name='pdbligand=CU:COPPER (II) ION'>CU</scene>	+	\|LIGAND= <scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>
	\|ACTIVITY=		\|ACTIVITY=
	\|GENE=		\|GENE=
		+	\|DOMAIN=
		+	\|RELATEDENTRY=
		+	\|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1hc6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hc6 OCA], [http://www.ebi.ac.uk/pdbsum/1hc6 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1hc6 RCSB]</span>
	}}		}}

Line 24:		Line 27:
	[[Category: Hol, W G.J.]]		[[Category: Hol, W G.J.]]
	[[Category: Volbeda, A.]]		[[Category: Volbeda, A.]]
-	[[Category: CU]]
	[[Category: oxygen transport]]		[[Category: oxygen transport]]

-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Thu~~ Mar ~~20 11~~:35:09 2008''	+	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:02:06 2008''

OCA at 09:35, 20 March 2008

2008-03-20T09:35:15Z

←Older revision		Revision as of 09:35, 20 March 2008
Line 1:		Line 1:
-	[[Image:1hc6.jpg\|left\|200px]]~~<br /><applet load~~="1hc6~~" size~~="350~~" color~~=~~"white" frame~~=~~"true" align="right" spinBox="true"~~	+	[[Image:1hc6.jpg\|left\|200px]]
-	~~caption="~~1hc6, resolution 3.2Å" />	+
-	'''CRYSTAL STRUCTURE OF HEXAMERIC HAEMOCYANIN FROM PANULIRUS INTERRUPTUS REFINED AT 3.2 ANGSTROMS RESOLUTION'''~~<br />~~	+	{{Structure
		+	\|PDB= 1hc6 \|SIZE=350\|CAPTION= <scene name='initialview01'>1hc6</scene>, resolution 3.2Å
		+	\|SITE=
		+	\|LIGAND= <scene name='pdbligand=CU:COPPER (II) ION'>CU</scene>
		+	\|ACTIVITY=
		+	\|GENE=
		+	}}
		+
		+	'''CRYSTAL STRUCTURE OF HEXAMERIC HAEMOCYANIN FROM PANULIRUS INTERRUPTUS REFINED AT 3.2 ANGSTROMS RESOLUTION'''
		+

	==Overview==		==Overview==
Line 7:		Line 16:

	==About this Structure==		==About this Structure==
-	1HC6 is a [~~http://en.wikipedia.org/wiki/Single_protein~~ Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Panulirus_interruptus Panulirus interruptus~~] with <scene name='pdbligand=CU:'>CU</scene> as [http://en.wikipedia.org/wiki/ligand ligand~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HC6 OCA].	+	1HC6 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Panulirus_interruptus Panulirus interruptus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HC6 OCA].

	==Reference==		==Reference==
-	Crystal structure of hexameric haemocyanin from Panulirus interruptus refined at 3.2 A resolution., Volbeda A, Hol WG, J Mol Biol. 1989 Sep 20;209(2):249-79. PMID:[http://~~ispc~~.~~weizmann~~.ac.~~il/~~/~~pmbin~~/~~getpm?pmid=~~2585484 2585484]	+	Crystal structure of hexameric haemocyanin from Panulirus interruptus refined at 3.2 A resolution., Volbeda A, Hol WG, J Mol Biol. 1989 Sep 20;209(2):249-79. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/2585484 2585484]
	[[Category: Panulirus interruptus]]		[[Category: Panulirus interruptus]]
	[[Category: Single protein]]		[[Category: Single protein]]
Line 18:		Line 27:
	[[Category: oxygen transport]]		[[Category: oxygen transport]]

-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu ~~Feb 21 12~~:59:41 2008''	+	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:35:09 2008''

OCA at 10:59, 21 February 2008

2008-02-21T10:59:42Z

←Older revision		Revision as of 10:59, 21 February 2008
Line 1:		Line 1:
-	[[Image:1hc6.jpg\|left\|200px]]<br /><applet load="1hc6" size="~~450~~" color="white" frame="true" align="right" spinBox="true"	+	[[Image:1hc6.jpg\|left\|200px]]<br /><applet load="1hc6" size="350" color="white" frame="true" align="right" spinBox="true"
	caption="1hc6, resolution 3.2Å" />		caption="1hc6, resolution 3.2Å" />
	'''CRYSTAL STRUCTURE OF HEXAMERIC HAEMOCYANIN FROM PANULIRUS INTERRUPTUS REFINED AT 3.2 ANGSTROMS RESOLUTION'''<br />		'''CRYSTAL STRUCTURE OF HEXAMERIC HAEMOCYANIN FROM PANULIRUS INTERRUPTUS REFINED AT 3.2 ANGSTROMS RESOLUTION'''<br />

	==Overview==		==Overview==
-	The use of non-crystallographic symmetry restraints in the refinement of, the haemocyanin hexamer from Panulirus interruptus at 3.2 A resolution has, resulted in a final model with a very reasonable geometry and a, crystallographic R-factor of 20.1%, using 59,193 observed structure factor, amplitudes between 8.0 and 3.2 A. The mean co-ordinate error is, approximately 0.35 A. The six subunits appear to be related by symmetry, operations that differ slightly from 32 point group symmetry. The six, subunits have essentially maintained the same structure. The hexamer, with, point group 32, is best described as a trimer of "tight dimers". The, contacts between the subunits in such a dimer are more numerous, and, better conserved during evolution than contacts in a trimer. The interface, of a tight dimer is separated by an internal cavity into two "contact, areas". The contact area nearest to the centre of the hexamer is most, extensive and consists mainly of residues that are quite conserved among, arthropodan haemocyanins. All these residues are provided by the second, domain of each subunit. Hence, this second domain may play a crucial role, in the allosteric functioning of this oxygen transport protein. The, dinuclear copper oxygen-binding site resides in the centre of domain 2., This oxygen-binding centre is not fully accessible from the solvent. Three, large cavities occur, however, within each subunit at the interfaces of, the three domains. All three cavities contain ordered water molecules, and, two of them are accessible from the surrounding solvent. These cavities, may play a role in facilitating fast movement of dioxygen towards the, binding site, which is situated in a highly conserved, rather hydrophobic, core. A detailed definition of the geometry of the copper site is, of, course, not possible at the limited resolution of 3.2 A. Nevertheless, it, is possible to conclude that each copper is co-ordinated by two, more or, less tightly bound, histidine ligands and one more distant histidine, residue. The six histidine residues utilize their N epsilon atoms for, copper co-ordination, while their N delta atoms are engaged in hydrogen, bonds with conserved residues or water molecules. The two distant, histidine ligands are located in apical positions and are on opposite, sides with respect to the plane approximately defined by the four more, tightly bound histidine ligands and the two copper ions. The, copper-to-copper distance is 3.5 to 3.6 A in four of the subunits, but, this distance deviates considerably in two others.(ABSTRACT TRUNCATED AT, 400 WORDS)	+	The use of non-crystallographic symmetry restraints in the refinement of the haemocyanin hexamer from Panulirus interruptus at 3.2 A resolution has resulted in a final model with a very reasonable geometry and a crystallographic R-factor of 20.1%, using 59,193 observed structure factor amplitudes between 8.0 and 3.2 A. The mean co-ordinate error is approximately 0.35 A. The six subunits appear to be related by symmetry operations that differ slightly from 32 point group symmetry. The six subunits have essentially maintained the same structure. The hexamer, with point group 32, is best described as a trimer of "tight dimers". The contacts between the subunits in such a dimer are more numerous, and better conserved during evolution than contacts in a trimer. The interface of a tight dimer is separated by an internal cavity into two "contact areas". The contact area nearest to the centre of the hexamer is most extensive and consists mainly of residues that are quite conserved among arthropodan haemocyanins. All these residues are provided by the second domain of each subunit. Hence, this second domain may play a crucial role in the allosteric functioning of this oxygen transport protein. The dinuclear copper oxygen-binding site resides in the centre of domain 2. This oxygen-binding centre is not fully accessible from the solvent. Three large cavities occur, however, within each subunit at the interfaces of the three domains. All three cavities contain ordered water molecules, and two of them are accessible from the surrounding solvent. These cavities may play a role in facilitating fast movement of dioxygen towards the binding site, which is situated in a highly conserved, rather hydrophobic core. A detailed definition of the geometry of the copper site is, of course, not possible at the limited resolution of 3.2 A. Nevertheless, it is possible to conclude that each copper is co-ordinated by two, more or less tightly bound, histidine ligands and one more distant histidine residue. The six histidine residues utilize their N epsilon atoms for copper co-ordination, while their N delta atoms are engaged in hydrogen bonds with conserved residues or water molecules. The two distant histidine ligands are located in apical positions and are on opposite sides with respect to the plane approximately defined by the four more tightly bound histidine ligands and the two copper ions. The copper-to-copper distance is 3.5 to 3.6 A in four of the subunits, but this distance deviates considerably in two others.(ABSTRACT TRUNCATED AT 400 WORDS)

	==About this Structure==		==About this Structure==
-	1HC6 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Panulirus_interruptus Panulirus interruptus] with CU as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=1HC6 OCA].	+	1HC6 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Panulirus_interruptus Panulirus interruptus] with <scene name='pdbligand=CU:'>CU</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HC6 OCA].

	==Reference==		==Reference==
Line 13:		Line 13:
	[[Category: Panulirus interruptus]]		[[Category: Panulirus interruptus]]
	[[Category: Single protein]]		[[Category: Single protein]]
-	[[Category: Hol, W.G.J.]]	+	[[Category: Hol, W G.J.]]
	[[Category: Volbeda, A.]]		[[Category: Volbeda, A.]]
	[[Category: CU]]		[[Category: CU]]
	[[Category: oxygen transport]]		[[Category: oxygen transport]]

-	''Page seeded by [http://~~ispc~~.weizmann.ac.il/oca OCA ] on ~~Tue Nov 20 16~~:30:~~49 2007~~''	+	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:59:41 2008''

OCA: New page: 200px
'''CRYSTAL STRUCTURE OF ...
2007-11-20T14:23:37Z

New page: 200px<br /><applet load="1hc6" size="450" color="white" frame="true" align="right" spinBox="true" caption="1hc6, resolution 3.2Å" /> '''CRYSTAL STRUCTURE OF ...

New page
[[Image:1hc6.jpg|left|200px]]<br /><applet load="1hc6" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1hc6, resolution 3.2Å" />
'''CRYSTAL STRUCTURE OF HEXAMERIC HAEMOCYANIN FROM PANULIRUS INTERRUPTUS REFINED AT 3.2 ANGSTROMS RESOLUTION'''<br />

==Overview==
The use of non-crystallographic symmetry restraints in the refinement of, the haemocyanin hexamer from Panulirus interruptus at 3.2 A resolution has, resulted in a final model with a very reasonable geometry and a, crystallographic R-factor of 20.1%, using 59,193 observed structure factor, amplitudes between 8.0 and 3.2 A. The mean co-ordinate error is, approximately 0.35 A. The six subunits appear to be related by symmetry, operations that differ slightly from 32 point group symmetry. The six, subunits have essentially maintained the same structure. The hexamer, with, point group 32, is best described as a trimer of "tight dimers". The, contacts between the subunits in such a dimer are more numerous, and, better conserved during evolution than contacts in a trimer. The interface, of a tight dimer is separated by an internal cavity into two "contact, areas". The contact area nearest to the centre of the hexamer is most, extensive and consists mainly of residues that are quite conserved among, arthropodan haemocyanins. All these residues are provided by the second, domain of each subunit. Hence, this second domain may play a crucial role, in the allosteric functioning of this oxygen transport protein. The, dinuclear copper oxygen-binding site resides in the centre of domain 2., This oxygen-binding centre is not fully accessible from the solvent. Three, large cavities occur, however, within each subunit at the interfaces of, the three domains. All three cavities contain ordered water molecules, and, two of them are accessible from the surrounding solvent. These cavities, may play a role in facilitating fast movement of dioxygen towards the, binding site, which is situated in a highly conserved, rather hydrophobic, core. A detailed definition of the geometry of the copper site is, of, course, not possible at the limited resolution of 3.2 A. Nevertheless, it, is possible to conclude that each copper is co-ordinated by two, more or, less tightly bound, histidine ligands and one more distant histidine, residue. The six histidine residues utilize their N epsilon atoms for, copper co-ordination, while their N delta atoms are engaged in hydrogen, bonds with conserved residues or water molecules. The two distant, histidine ligands are located in apical positions and are on opposite, sides with respect to the plane approximately defined by the four more, tightly bound histidine ligands and the two copper ions. The, copper-to-copper distance is 3.5 to 3.6 A in four of the subunits, but, this distance deviates considerably in two others.(ABSTRACT TRUNCATED AT, 400 WORDS)

==About this Structure==
1HC6 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Panulirus_interruptus Panulirus interruptus] with CU as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1HC6 OCA].

==Reference==
Crystal structure of hexameric haemocyanin from Panulirus interruptus refined at 3.2 A resolution., Volbeda A, Hol WG, J Mol Biol. 1989 Sep 20;209(2):249-79. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=2585484 2585484]
[[Category: Panulirus interruptus]]
[[Category: Single protein]]
[[Category: Hol, W.G.J.]]
[[Category: Volbeda, A.]]
[[Category: CU]]
[[Category: oxygen transport]]

''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 16:30:49 2007''