1akd
From Proteopedia
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|PDB= 1akd |SIZE=350|CAPTION= <scene name='initialview01'>1akd</scene>, resolution 1.8Å | |PDB= 1akd |SIZE=350|CAPTION= <scene name='initialview01'>1akd</scene>, resolution 1.8Å | ||
|SITE= <scene name='pdbsite=HEM:Heme+Binding+Site'>HEM</scene> and <scene name='pdbsite=K:K++Binding+Site'>K</scene> | |SITE= <scene name='pdbsite=HEM:Heme+Binding+Site'>HEM</scene> and <scene name='pdbsite=K:K++Binding+Site'>K</scene> | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=CAM:CAMPHOR'>CAM</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</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=1akd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1akd OCA], [http://www.ebi.ac.uk/pdbsum/1akd PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1akd RCSB]</span> | ||
}} | }} | ||
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[[Category: Schlichting, I.]] | [[Category: Schlichting, I.]] | ||
[[Category: Schulze, H.]] | [[Category: Schulze, H.]] | ||
| - | [[Category: CAM]] | ||
| - | [[Category: HEM]] | ||
| - | [[Category: K]] | ||
[[Category: cytochrome p450]] | [[Category: cytochrome p450]] | ||
[[Category: electron transport]] | [[Category: electron transport]] | ||
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[[Category: oxygenase]] | [[Category: 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 18:42:06 2008'' |
Revision as of 15:42, 30 March 2008
| |||||||
| , resolution 1.8Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | and | ||||||
| Ligands: | , , | ||||||
| Activity: | Camphor 5-monooxygenase, with EC number 1.14.15.1 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CYTOCHROME P450CAM FROM PSEUDOMONAS PUTIDA, COMPLEXED WITH 1S-CAMPHOR
Overview
The crystal structure of cytochrome P-450cam complexed with the enantiomer (1S)-camphor has been solved to 1.8 angstroms resolution and compared with the structure of the (1R)-camphor P-450cam complex. The overall protein structure is the same for both enantiomer complexes. However, the orientation of the substrates in the heme pocket differs. In contrast to (1R)-camphor, the (1S)-enantiomer binds in at least two orientations. The major binding mode of (1S)-camphor resembles the one of the (1R)-enantiomer in that there is a hydrogen bond between Tyr-96 and the quinone group of camphor, and the 10-methyl group points towards the I-helix. The binding differs in that C-5 is not at a position suitable for hydroxylation. In the other orientation (1S)-camphor is not hydrogen bonded, but C-5 is located suitably for hydroxylation.
About this Structure
1AKD is a Single protein structure of sequence from Pseudomonas putida. Full crystallographic information is available from OCA.
Reference
Crystal structure of cytochrome P-450cam complexed with the (1S)-camphor enantiomer., Schlichting I, Jung C, Schulze H, FEBS Lett. 1997 Oct 6;415(3):253-7. PMID:9357977
Page seeded by OCA on Sun Mar 30 18:42:06 2008
