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PDBsum entry 7cpp

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Oxidoreductase(oxygenase) PDB id
7cpp
Contents
Protein chain
405 a.a.
Ligands
HEM
NCM
Waters ×206

References listed in PDB file
Key reference
Title The structural basis for substrate-Induced changes in redox potential and spin equilibrium in cytochrome p-450cam.
Authors R.Raag, T.L.Poulos.
Ref. Biochemistry, 1989, 28, 917-922. [DOI no: 10.1021/bi00428a077]
PubMed id 2713354
Abstract
The crystal structures of cytochrome P-450CAM complexed with the alternative substrates norcamphor and adamantanone have been refined at 2.0-A resolution and compared with the native, camphor-bound form of the enzyme. Norcamphor lacks the 8-, 9-, and 10-methyl groups of camphor. Thus, specific interactions between these groups and phenylalanine 87 and valines 247 and 295 are missing in the norcamphor complex. As a result, norcamphor binds about 0.9 A further from the oxygen-binding site than does camphor, which allows sufficient room for a water molecule or hydroxide ion to remain coordinated with the heme iron atom. The larger adamantanone occupies a position closer to that of camphor and, as in the camphor-bound enzyme, the heme iron remains pentacoordinate with no solvent molecule coordinated as a sixth ligand. A comparison of crystallographic temperature factors indicates that norcamphor is more "loosely" bound than are either camphor or adamantanone, as might be expected from the relative sizes of the different substrates. The looser fit of norcamphor in the active-site pocket results in a less specific pattern of hydroxylation. The presence of an aqua ligand is the likely structural basis for the norcamphor-P-450CAM complex having both a lower redox potential and higher percentage of low-spin heme than do either the camphor-P-450CAM or adamantanone-P-450CAM complexes.
Secondary reference #1
Title X-Ray crystallographic structural studies of cytochrome p-450=CAM=+
Authors R.Raag, T.L.Poulos.
Ref. TO BE PUBLISHED ...
Secondary reference #2
Title Crystal structures of cytochrome p-450cam complexed with camphane, Thiocamphor, And adamantane: factors controlling p-450 substrate hydroxylation.
Authors R.Raag, T.L.Poulos.
Ref. Biochemistry, 1991, 30, 2674-2684. [DOI no: 10.1021/bi00224a016]
PubMed id 2001355
Full text Abstract
Secondary reference #3
Title Crystal structure of the carbon monoxide-Substrate-Cytochrome p-450cam ternary complex.
Authors R.Raag, T.L.Poulos.
Ref. Biochemistry, 1989, 28, 7586-7592.
PubMed id 2611203
Abstract
PROCHECK
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