3sdp

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[[Image:3sdp.jpg|left|200px]]<br /><applet load="3sdp" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:3sdp.jpg|left|200px]]
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caption="3sdp, resolution 2.1&Aring;" />
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'''THE 2.1 ANGSTROMS RESOLUTION STRUCTURE OF IRON SUPEROXIDE DISMUTASE FROM PSEUDOMONAS OVALIS'''<br />
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{{Structure
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|PDB= 3sdp |SIZE=350|CAPTION= <scene name='initialview01'>3sdp</scene>, resolution 2.1&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=FE:FE (III) ION'>FE</scene>
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|ACTIVITY= [http://en.wikipedia.org/wiki/Superoxide_dismutase Superoxide dismutase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.15.1.1 1.15.1.1]
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|GENE=
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}}
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'''THE 2.1 ANGSTROMS RESOLUTION STRUCTURE OF IRON SUPEROXIDE DISMUTASE FROM PSEUDOMONAS OVALIS'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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3SDP is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pseudomonas_putida Pseudomonas putida] with <scene name='pdbligand=FE:'>FE</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. The following page contains interesting information on the relation of 3SDP with [[http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb94_1.html Superoxide Dismutase]]. Active as [http://en.wikipedia.org/wiki/Superoxide_dismutase Superoxide dismutase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.15.1.1 1.15.1.1] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3SDP OCA].
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3SDP is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Pseudomonas_putida Pseudomonas putida]. The following page contains interesting information on the relation of 3SDP with [[http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb94_1.html Superoxide Dismutase]]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3SDP OCA].
==Reference==
==Reference==
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The 2.1-A resolution structure of iron superoxide dismutase from Pseudomonas ovalis., Stoddard BL, Howell PL, Ringe D, Petsko GA, Biochemistry. 1990 Sep 25;29(38):8885-93. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=2271564 2271564]
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The 2.1-A resolution structure of iron superoxide dismutase from Pseudomonas ovalis., Stoddard BL, Howell PL, Ringe D, Petsko GA, Biochemistry. 1990 Sep 25;29(38):8885-93. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/2271564 2271564]
[[Category: Pseudomonas putida]]
[[Category: Pseudomonas putida]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: oxidoreductase (superoxide acceptor)]]
[[Category: oxidoreductase (superoxide acceptor)]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 19:11:17 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 19:07:12 2008''

Revision as of 17:07, 20 March 2008


PDB ID 3sdp

Drag the structure with the mouse to rotate
, resolution 2.1Å
Ligands:
Activity: Superoxide dismutase, with EC number 1.15.1.1
Coordinates: save as pdb, mmCIF, xml



THE 2.1 ANGSTROMS RESOLUTION STRUCTURE OF IRON SUPEROXIDE DISMUTASE FROM PSEUDOMONAS OVALIS


Overview

The 2.1-A resolution crystal structure of native uncomplexed iron superoxide dismutase (EC 1.15.1.1) from Pseudomonas ovalis was solved and refined to a final R factor of 24%. The dimeric structure contains one catalytic iron center per monomer with an asymmetric trigonal-bipyramidal coordination of protein ligands to the metal. Each monomer contains two domains, with the trigonal ligands (histidines 74 and 160; aspartate 156) contributed by the large domain and stabilized by an extended hydrogen-bonded network, including residues from opposing monomers. The axial ligand (histidine 26) is found on the small domain and does not participate extensively in the stabilizing H-bond network. The open axial coordination position of the iron is devoid of bound water molecules or anions. The metal is located 0.5 A out of the plane of the trigonal ligands toward histidine 26, providing a slightly skewed coordination away from the iron binding site. The molecule contains a glutamine residue in the active site which is conserved between all iron enzymes sequenced to data but which is conserved among all manganese SODs at a separate position in the sequence. This residue shows the same structural interactions in both cases, implying that iron and manganese SODs are second-site revertants of one another.

About this Structure

3SDP is a Single protein structure of sequence from Pseudomonas putida. The following page contains interesting information on the relation of 3SDP with [Superoxide Dismutase]. Full crystallographic information is available from OCA.

Reference

The 2.1-A resolution structure of iron superoxide dismutase from Pseudomonas ovalis., Stoddard BL, Howell PL, Ringe D, Petsko GA, Biochemistry. 1990 Sep 25;29(38):8885-93. PMID:2271564

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