This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.

1o76

From Proteopedia

(Difference between revisions)

Jump to: navigation, search

Revision as of 07:12, 7 February 2018

CYANIDE COMPLEX OF P450CAM FROM PSEUDOMONAS PUTIDA

Structural highlights

1o76 is a 2 chain structure with sequence from "bacillus_fluorescens_putidus"_flugge_1886 "bacillus fluorescens putidus" flugge 1886. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	, , , ,
Related:	1akd, 1c8j, 1cp4, 1dz4, 1dz6, 1dz8, 1dz9, 1geb, 1gek, 1gem, 1gjm, 1iwi, 1iwj, 1iwk, 1j51, 1k2o, 1mpw, 1noo, 1pha, 1phb, 1phc, 1phd, 1phe, 1phf, 1phg, 1qmq, 2cp4, 2cpp, 3cp4, 3cpp, 4cp4, 4cpp, 5cp4, 5cpp, 6cp4, 6cpp, 7cpp, 8cpp
Activity:	Camphor 5-monooxygenase, with EC number 1.14.15.1
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[CPXA_PSEPU] Involved in a camphor oxidation system.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

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.

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^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Fedorov R, Ghosh DK, Schlichting I. Crystal structures of cyanide complexes of P450cam and the oxygenase domain of inducible nitric oxide synthase-structural models of the short-lived oxygen complexes. Arch Biochem Biophys. 2003 Jan 1;409(1):25-31. PMID:12464241

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1o76"

@@ Line 1: / Line 1: @@
 ==CYANIDE COMPLEX OF P450CAM FROM PSEUDOMONAS PUTIDA==
 <StructureSection load='1o76' size='340' side='right' caption='[[1o76]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
@@ Line 6: / Line 7: @@
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1akd|1akd]], [[1c8j|1c8j]], [[1cp4|1cp4]], [[1dz4|1dz4]], [[1dz6|1dz6]], [[1dz8|1dz8]], [[1dz9|1dz9]], [[1geb|1geb]], [[1gek|1gek]], [[1gem|1gem]], [[1gjm|1gjm]], [[1iwi|1iwi]], [[1iwj|1iwj]], [[1iwk|1iwk]], [[1j51|1j51]], [[1k2o|1k2o]], [[1mpw|1mpw]], [[1noo|1noo]], [[1pha|1pha]], [[1phb|1phb]], [[1phc|1phc]], [[1phd|1phd]], [[1phe|1phe]], [[1phf|1phf]], [[1phg|1phg]], [[1qmq|1qmq]], [[2cp4|2cp4]], [[2cpp|2cpp]], [[3cp4|3cp4]], [[3cpp|3cpp]], [[4cp4|4cp4]], [[4cpp|4cpp]], [[5cp4|5cp4]], [[5cpp|5cpp]], [[6cp4|6cp4]], [[6cpp|6cpp]], [[7cpp|7cpp]], [[8cpp|8cpp]]</td></tr>
 <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><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></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><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://pdbe.org/1o76 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1o76 RCSB], [http://www.ebi.ac.uk/pdbsum/1o76 PDBsum]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><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://pdbe.org/1o76 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1o76 RCSB], [http://www.ebi.ac.uk/pdbsum/1o76 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1o76 ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 14: / Line 15: @@
 Check<jmol>
   <jmolCheckbox>
-    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/o7/1o76_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/o7/1o76_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
@@ Line 29: / Line 30: @@
 </div>
 <div class="pdbe-citations 1o76" style="background-color:#fffaf0;"></div>
-==See Also==
-*[[Cytochrome P450|Cytochrome P450]]
 == References ==
 <references/>

1o76

From Proteopedia

Revision as of 07:12, 7 February 2018

CYANIDE COMPLEX OF P450CAM FROM PSEUDOMONAS PUTIDA

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox