2j5m
From Proteopedia
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|PDB= 2j5m |SIZE=350|CAPTION= <scene name='initialview01'>2j5m</scene>, resolution 1.75Å | |PDB= 2j5m |SIZE=350|CAPTION= <scene name='initialview01'>2j5m</scene>, resolution 1.75Å | ||
|SITE= <scene name='pdbsite=AC1:Act+Binding+Site+For+Chain+A'>AC1</scene> | |SITE= <scene name='pdbsite=AC1:Act+Binding+Site+For+Chain+A'>AC1</scene> | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=PCA:PYROGLUTAMIC+ACID'>PCA</scene>, <scene name='pdbligand=PEO:HYDROGEN+PEROXIDE'>PEO</scene> |
| - | + | |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= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2j5m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2j5m OCA], [http://www.ebi.ac.uk/pdbsum/2j5m PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2j5m RCSB]</span> | ||
}} | }} | ||
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[[Category: Shaik, S.]] | [[Category: Shaik, S.]] | ||
[[Category: Terner, J.]] | [[Category: Terner, J.]] | ||
| - | [[Category: ACT]] | ||
| - | [[Category: EDO]] | ||
| - | [[Category: HEM]] | ||
| - | [[Category: MAN]] | ||
| - | [[Category: MN]] | ||
| - | [[Category: NAG]] | ||
| - | [[Category: PEO]] | ||
[[Category: chloride]] | [[Category: chloride]] | ||
[[Category: glycoprotein]] | [[Category: glycoprotein]] | ||
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[[Category: pyrrolidone carboxylic acid]] | [[Category: pyrrolidone carboxylic acid]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 03:53:15 2008'' |
Revision as of 00:53, 31 March 2008
| |||||||
| , resolution 1.75Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | |||||||
| Ligands: | , , , , , , , , | ||||||
| Activity: | Chloride peroxidase, with EC number 1.11.1.10 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
STRUCTURE OF CHLOROPEROXIDASE COMPOUND 0
Overview
We have determined the crystal structure of the chloroperoxidase (CPO) hydroperoxo reaction intermediate (CPO compound 0) at 1.75-A resolution. The intermediate was generated through controlled photoreduction of the CPO oxygen complex during x-ray data collection, which was monitored by recording of the crystal absorption spectra. Initially, the peroxo-anion species was formed and then protonated to yield compound 0. Quantum chemical calculations indicate that the peroxo-anion species is not stable and collapses instantaneously to compound 0. Compound 0 is present in the ferric low-spin doublet ground state and is characterized by a long O O bond length of 1.5 A and a Fe O bond distance of 1.8 A, which is also observed in the crystal structure.
About this Structure
2J5M is a Single protein structure of sequence from Leptoxyphium fumago. Full crystallographic information is available from OCA.
Reference
Structure and quantum chemical characterization of chloroperoxidase compound 0, a common reaction intermediate of diverse heme enzymes., Kuhnel K, Derat E, Terner J, Shaik S, Schlichting I, Proc Natl Acad Sci U S A. 2007 Jan 2;104(1):99-104. Epub 2006 Dec 26. PMID:17190816
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