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1DZ9

Putative oxo complex of P450cam from Pseudomonas putida

Summary for 1DZ9
Entry DOI10.2210/pdb1dz9/pdb
Related1AKD 1CP4 1DZ4 1DZ6 1DZ8 1NOO 1PHA 1PHB 1PHC 1PHD 1PHE 1PHF 1PHG 2CP4 2CPP 3CP4 3CPP 4CP4 4CPP 5CP4 5CPP 6CP4 6CPP 7CPP 8CPP
DescriptorCYTOCHROME P450-CAM, PROTOPORPHYRIN IX CONTAINING FE, OXYGEN ATOM, ... (7 entities in total)
Functional Keywordsoxidoreductase, mono-oxygenase, heme, reaction intermediate
Biological sourcePSEUDOMONAS PUTIDA
Total number of polymer chains2
Total formula weight94968.67
Authors
Schlichting, I.,Berendzen, J.,Chu, K.,Stock, A.M.,Maves, S.A.,Benson, D.E.,Sweet, R.M.,Ringe, D.,Petsko, G.A.,Sligar, S.G. (deposition date: 2000-02-18, release date: 2000-03-30, Last modification date: 2024-05-08)
Primary citationSchlichting, I.,Berendzen, J.,Chu, K.,Stock, A.M.,Maves, S.A.,Benson, D.E.,Sweet, R.M.,Ringe, D.,Petsko, G.A.,Sligar, S.G.
The Catalytic Pathway of Cytochrome P450Cam at Atomic Resolution
Science, 287:1615-, 2000
Cited by
PubMed Abstract: Members of the cytochrome P450 superfamily catalyze the addition of molecular oxygen to nonactivated hydrocarbons at physiological temperature-a reaction that requires high temperature to proceed in the absence of a catalyst. Structures were obtained for three intermediates in the hydroxylation reaction of camphor by P450cam with trapping techniques and cryocrystallography. The structure of the ferrous dioxygen adduct of P450cam was determined with 0.91 angstrom wavelength x-rays; irradiation with 1.5 angstrom x-rays results in breakdown of the dioxygen molecule to an intermediate that would be consistent with an oxyferryl species. The structures show conformational changes in several important residues and reveal a network of bound water molecules that may provide the protons needed for the reaction.
PubMed: 10698731
DOI: 10.1126/SCIENCE.287.5458.1615
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.9 Å)
Structure validation

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