2hpd
From Proteopedia
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| , resolution 2.0Å | |||||||
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| Ligands: | |||||||
| Activity: | Unspecific monooxygenase, with EC number 1.14.14.1 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CRYSTAL STRUCTURE OF HEMOPROTEIN DOMAIN OF P450BM-3, A PROTOTYPE FOR MICROSOMAL P450'S
Overview
Cytochrome P450BM-3, a bacterial fatty acid monoxygenase, resembles the eukaryotic microsomal P450's and their flavoprotein reductase in primary structure and function. The three-dimensional structure of the hemoprotein domain of P450BM-3 was determined by x-ray diffraction and refined to an R factor of 16.9 percent at 2.0 angstrom resolution. The structure consists of an alph and a beta domain. The active site heme is accessible through a long hydrophobic channel formed primarily by the beta domain and the B' and F helices of the alpha domain. The two molecules in the asymmetric unit differ in conformation around the substrate binding pocket. Substantial differences between P450BM-3 and P450cam, the only other P450 structure available, are observed around the substrate binding pocket and the regions important for redox partner binding. A general mechanism for proton transfer in P450's is also proposed.
About this Structure
2HPD is a Single protein structure of sequence from Bacillus megaterium. Full crystallographic information is available from OCA.
Reference
Crystal structure of hemoprotein domain of P450BM-3, a prototype for microsomal P450's., Ravichandran KG, Boddupalli SS, Hasermann CA, Peterson JA, Deisenhofer J, Science. 1993 Aug 6;261(5122):731-6. PMID:8342039
Page seeded by OCA on Mon Mar 31 03:33:29 2008
