1a88
From Proteopedia
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|SITE= <scene name='pdbsite=CTA:Catalytic+Triad,+Chain+A'>CTA</scene>, <scene name='pdbsite=CTB:Catalytic+Triad,+Chain+B'>CTB</scene> and <scene name='pdbsite=CTC:Catalytic+Triad,+Chain+C'>CTC</scene> | |SITE= <scene name='pdbsite=CTA:Catalytic+Triad,+Chain+A'>CTA</scene>, <scene name='pdbsite=CTB:Catalytic+Triad,+Chain+B'>CTB</scene> and <scene name='pdbsite=CTC:Catalytic+Triad,+Chain+C'>CTC</scene> | ||
|LIGAND= | |LIGAND= | ||
| - | |ACTIVITY= [http://en.wikipedia.org/wiki/Chloride_peroxidase Chloride peroxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.11.1.10 1.11.1.10] | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Chloride_peroxidase Chloride peroxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.11.1.10 1.11.1.10] </span> |
|GENE= CPO-L ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1916 Streptomyces lividans]) | |GENE= CPO-L ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1916 Streptomyces lividans]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1a88 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1a88 OCA], [http://www.ebi.ac.uk/pdbsum/1a88 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1a88 RCSB]</span> | ||
}} | }} | ||
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[[Category: oxidoreductase]] | [[Category: oxidoreductase]] | ||
| - | ''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 18:35:21 2008'' |
Revision as of 15:35, 30 March 2008
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| , resolution 1.90Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | , and | ||||||
| Gene: | CPO-L (Streptomyces lividans) | ||||||
| Activity: | Chloride peroxidase, with EC number 1.11.1.10 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CHLOROPEROXIDASE L
Overview
The structures of cofactor-free haloperoxidases from Streptomyces aureofaciens, Streptomyces lividans, and Pseudomonas fluorescens have been determined at resolutions between 1.9 A and 1.5 A. The structures of two enzymes complexed with benzoate or propionate identify the binding site for the organic acids which are required for the haloperoxidase activity. Based on these complexes and on the structure of an inactive variant, a reaction mechanism is proposed for the halogenation reaction with peroxoacid and hypohalous acid as reaction intermediates. Comparison of the structures suggests that a specific halide binding site is absent in the enzymes but that hydrophobic organic compounds may fit into the active site pocket for halogenation at preferential sites.
About this Structure
1A88 is a Single protein structure of sequence from Streptomyces lividans. Full crystallographic information is available from OCA.
Reference
Structural investigation of the cofactor-free chloroperoxidases., Hofmann B, Tolzer S, Pelletier I, Altenbuchner J, van Pee KH, Hecht HJ, J Mol Biol. 1998 Jun 19;279(4):889-900. PMID:9642069
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