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1mba

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Revision as of 09:25, 5 May 2021

APLYSIA LIMACINA MYOGLOBIN. CRYSTALLOGRAPHIC ANALYSIS AT 1.6 ANGSTROMS RESOLUTION

Structural highlights

1mba is a 1 chain structure with sequence from Aplli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
NonStd Res:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

The crystal structure of the ferric form of myoglobin from the mollusc Aplysia limacina has been refined at 1.6 A resolution, by restrained crystallographic refinement methods. The crystallographic R-factor is 0.19. The tertiary structure of the molecule conforms to the common globin fold, consisting of eight alpha-helices. The N-terminal helix A and helix G deviate significantly from linearity. The distal residue is recognized as Val63 (E7), which, however, does not contact the heme directly. Moreover the sixth (distal) co-ordination position of heme iron is not occupied by a water molecule at neutrality, i.e. below the acid-alkaline transition point of A. limacina myoglobin. The heme group sits in its crevice in the conventional orientation and no signs of heme isomerism are evident. The iron atom is 0.26 A out of the porphyrin plane, with a mean Fe-N (porphyrin) distance of 2.01 A. The co-ordination bond to the proximal histidine has a length of 2.05 A, and forms an angle of 4 degrees with the heme normal. A plane containing the imidazole ring of the proximal His intersects the heme at an angle of 29 degrees with the (porphyrin) 4N-2N direction. Inspection of the structure of pH 9.0 indicates that a hydroxyl ion is bound to the Fe sixth co-ordination position.

Aplysia limacina myoglobin. Crystallographic analysis at 1.6 A resolution.,Bolognesi M, Onesti S, Gatti G, Coda A, Ascenzi P, Brunori M J Mol Biol. 1989 Feb 5;205(3):529-44. PMID:2926816^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Bolognesi M, Onesti S, Gatti G, Coda A, Ascenzi P, Brunori M. Aplysia limacina myoglobin. Crystallographic analysis at 1.6 A resolution. J Mol Biol. 1989 Feb 5;205(3):529-44. PMID:2926816

1 Structural highlights
2 Evolutionary Conservation
3 Publication Abstract from PubMed
4 See Also
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1mba"

@@ Line 3: / Line 3: @@
 <StructureSection load='1mba' size='340' side='right'caption='[[1mba]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1mba]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Aplli Aplli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MBA OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1MBA FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1mba]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Aplli Aplli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MBA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1MBA FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene></td></tr>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene></td></tr>
 <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1mba FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mba OCA], [http://pdbe.org/1mba PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1mba RCSB], [http://www.ebi.ac.uk/pdbsum/1mba PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1mba ProSAT]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1mba FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mba OCA], [https://pdbe.org/1mba PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1mba RCSB], [https://www.ebi.ac.uk/pdbsum/1mba PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1mba ProSAT]</span></td></tr>
 </table>
 == Evolutionary Conservation ==
@@ Line 29: / Line 29: @@
 ==See Also==
-*[[Myoglobin|Myoglobin]]
+*[[Myoglobin 3D structures|Myoglobin 3D structures]]
 == References ==
 <references/>

1mba

From Proteopedia

Revision as of 09:25, 5 May 2021

APLYSIA LIMACINA MYOGLOBIN. CRYSTALLOGRAPHIC ANALYSIS AT 1.6 ANGSTROMS RESOLUTION

Structural highlights

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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