1phc
From Proteopedia
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|PDB= 1phc |SIZE=350|CAPTION= <scene name='initialview01'>1phc</scene>, resolution 1.6Å | |PDB= 1phc |SIZE=350|CAPTION= <scene name='initialview01'>1phc</scene>, resolution 1.6Å | ||
|SITE= | |SITE= | ||
- | |LIGAND= <scene name='pdbligand=HEM:PROTOPORPHYRIN IX CONTAINING FE'>HEM</scene> | + | |LIGAND= <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</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=1phc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1phc OCA], [http://www.ebi.ac.uk/pdbsum/1phc PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1phc RCSB]</span> | ||
}} | }} | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Poulos, T L.]] | [[Category: Poulos, T L.]] | ||
- | [[Category: HEM]] | ||
[[Category: oxidoreductase(oxygenase)]] | [[Category: oxidoreductase(oxygenase)]] | ||
- | ''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 22:59:42 2008'' |
Revision as of 19:59, 30 March 2008
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, resolution 1.6Å | |||||||
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Ligands: | |||||||
Activity: | Camphor 5-monooxygenase, with EC number 1.14.15.1 | ||||||
Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
Coordinates: | save as pdb, mmCIF, xml |
CRYSTAL STRUCTURE OF SUBSTRATE-FREE PSEUDOMONAS PUTIDA CYTOCHROME P450
Overview
The crystal structure of Pseudomonas putida cytochrome P-450cam in the substrate-free form has been refined at 2.20-A resolution and compared to the substrate-bound form of the enzyme. In the absence of the substrate camphor, the P-450cam heme iron atom is hexacoordinate with the sulfur atom of Cys-357 providing one axial heme ligand and a water molecule or hydroxide ion providing the other axial ligand. A network of hydrogen-bonded solvent molecules occupies the substrate pocket in addition to the iron-linked aqua ligand. When a camphor molecule binds, the active site waters including the aqua ligand are displaced, resulting in a pentacoordinate high-spin heme iron atom. Analysis of the Fno camphor - F camphor difference Fourier and a quantitative comparison of the two refined structures reveal that no detectable conformational change results from camphor binding other than a small repositioning of a phenylalanine side chain that contacts the camphor molecule. However, large decreases in the mean temperature factors of three separate segments of the protein centered on Tyr-96, Thr-185, and Asp-251 result from camphor binding. This indicates that camphor binding decreases the flexibility in these three regions of the P-450cam molecule without altering the mean position of the atoms involved.
About this Structure
1PHC is a Single protein structure of sequence from Pseudomonas putida. Full crystallographic information is available from OCA.
Reference
Crystal structure of substrate-free Pseudomonas putida cytochrome P-450., Poulos TL, Finzel BC, Howard AJ, Biochemistry. 1986 Sep 9;25(18):5314-22. PMID:3768350
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