1dcc
From Proteopedia
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|PDB= 1dcc |SIZE=350|CAPTION= <scene name='initialview01'>1dcc</scene>, resolution 2.2Å | |PDB= 1dcc |SIZE=350|CAPTION= <scene name='initialview01'>1dcc</scene>, resolution 2.2Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=OXY:OXYGEN+MOLECULE'>OXY</scene> |
| - | |ACTIVITY= [http://en.wikipedia.org/wiki/Cytochrome-c_peroxidase Cytochrome-c peroxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.11.1.5 1.11.1.5] | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Cytochrome-c_peroxidase Cytochrome-c peroxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.11.1.5 1.11.1.5] </span> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1dcc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dcc OCA], [http://www.ebi.ac.uk/pdbsum/1dcc PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1dcc RCSB]</span> | ||
}} | }} | ||
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[[Category: Miller, M A.]] | [[Category: Miller, M A.]] | ||
[[Category: Shaw, A.]] | [[Category: Shaw, A.]] | ||
| - | [[Category: HEM]] | ||
| - | [[Category: OXY]] | ||
[[Category: oxidoreductase(h2o2(a))]] | [[Category: oxidoreductase(h2o2(a))]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:38:49 2008'' |
Revision as of 16:38, 30 March 2008
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| , resolution 2.2Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Activity: | Cytochrome-c peroxidase, with EC number 1.11.1.5 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
2.2 ANGSTROM STRUCTURE OF OXYPEROXIDASE: A MODEL FOR THE ENZYME:PEROXIDE COMPLEX
Overview
The Fe+3-OOH complex of peroxidases has a very short half life, and its structure cannot be determined by conventional methods. The Fe+2-O2 complex provides a useful structural model for this intermediate, as it differs by only one electron and one proton from the transient Fe+3-OOH complex. We therefore determined the crystal structure of the Fe+2-O2 complex formed by a yeast cytochrome c peroxidase mutant with Trp 191 replaced by Phe. The refined structure shows that dioxygen can form a hydrogen bond with the conserved distal His residue, but not with the conserved distal Arg residue. When the transient Fe+3-OOH complex is modelled in a similar orientation, the active site of peroxidase appears to be optimized for catalysing proton transfer between the vicinal oxygen atoms of the peroxy-anion.
About this Structure
1DCC is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.
Reference
2.2 A structure of oxy-peroxidase as a model for the transient enzyme: peroxide complex., Miller MA, Shaw A, Kraut J, Nat Struct Biol. 1994 Aug;1(8):524-31. PMID:7664080
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