1o76
From Proteopedia
| Line 4: | Line 4: | ||
|PDB= 1o76 |SIZE=350|CAPTION= <scene name='initialview01'>1o76</scene>, resolution 1.8Å | |PDB= 1o76 |SIZE=350|CAPTION= <scene name='initialview01'>1o76</scene>, resolution 1.8Å | ||
|SITE= <scene name='pdbsite=AC1:K+Binding+Site+For+Chain+B'>AC1</scene> | |SITE= <scene name='pdbsite=AC1:K+Binding+Site+For+Chain+B'>AC1</scene> | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=CAM:CAMPHOR'>CAM</scene>, <scene name='pdbligand=CYN:CYANIDE+ION'>CYN</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene> |
| - | |ACTIVITY= [http://en.wikipedia.org/wiki/Camphor_5-monooxygenase Camphor 5-monooxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.15.1 1.14.15.1] | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Camphor_5-monooxygenase Camphor 5-monooxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.15.1 1.14.15.1] </span> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1o76 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1o76 OCA], [http://www.ebi.ac.uk/pdbsum/1o76 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1o76 RCSB]</span> | ||
}} | }} | ||
| Line 26: | Line 29: | ||
[[Category: Ghosh, D.]] | [[Category: Ghosh, D.]] | ||
[[Category: Schlichting, I.]] | [[Category: Schlichting, I.]] | ||
| - | [[Category: CAM]] | ||
| - | [[Category: CYN]] | ||
| - | [[Category: HEM]] | ||
| - | [[Category: K]] | ||
| - | [[Category: TRS]] | ||
[[Category: electron transport]] | [[Category: electron transport]] | ||
[[Category: heme]] | [[Category: heme]] | ||
| Line 36: | Line 34: | ||
[[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 22:40:52 2008'' |
Revision as of 19:40, 30 March 2008
| |||||||
| , resolution 1.8Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | |||||||
| Ligands: | , , , , | ||||||
| Activity: | Camphor 5-monooxygenase, with EC number 1.14.15.1 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CYANIDE COMPLEX OF P450CAM FROM PSEUDOMONAS PUTIDA
Overview
The crystal structure of the ternary cyanide complex of P450cam and camphor was determined to 1.8A resolution and found to be identical with the structure of the active oxygen complex [I. Schlichting et al., 2000, Science 287, 1615]. Notably, cyanide binds in a bent mode and induces the active conformation that is characterized by the presence of two water molecules and a flip of the carbonyl of the conserved Asp251. The structure of the ternary complex of cyanide, L-arginine, and the oxygenase domain of inducible nitric oxide synthase was determined to 2.4A resolution. Cyanide binds essentially linearly, interacts with L-Arg, and induces the binding of a water molecule at the active site. This water is positioned by backbone interactions, located 2.8A from the nitrogen atom of cyanide, and could provide a proton required for O-O bond scission in the hydroxylation reaction of nitric oxide synthase.
About this Structure
1O76 is a Single protein structure of sequence from Pseudomonas putida. Full crystallographic information is available from OCA.
Reference
Crystal structures of cyanide complexes of P450cam and the oxygenase domain of inducible nitric oxide synthase-structural models of the short-lived oxygen complexes., Fedorov R, Ghosh DK, Schlichting I, Arch Biochem Biophys. 2003 Jan 1;409(1):25-31. PMID:12464241
Page seeded by OCA on Sun Mar 30 22:40:52 2008
