Structure of PDB 1jme Chain B

Receptor sequence
>1jmeB (length=441) Species: 1404 (Priestia megaterium) [Search protein sequence]
KEMPQPKTFGELKNLPLLNTDKPVQALMKIADELGEIFKFEAPGRVTRYL
SSQRLIKEACDESRFDKNLSQALKFVRDFAGDGLFTSWTHEKNWKKAHNI
LLPSFSQQAMKGYHAMMVDIAVQLVQKWERLNADEHIEVPEDMTRLTLDT
IGLCGFNYRFNSFYRDQPHPFITSMVRALDEAMNKLNKRQFQEDIKVMND
LVDKIIADRKASGEQSDDLLTHMLNGKDPETGEPLDDENIRYQIITFLIA
GHETTSGLLSFALYFLVKNPHVLQKAAEEAARVLVDPVPSYKQVKQLKYV
GMVLNEALRLWPTAPAFSLYAKEDTVLGGEYPLEKGDELMVLIPQLHRDK
TIWGDDVEEFRPERFENPSAIPQHAFKPHGNGQRACIGQQFALHEATLVL
GMMLKHFDFEDHTNYELDIKETLTLKPEGFVVKAKSKKIPL
3D structure
PDB1jme Structural and spectroscopic analysis of the F393H mutant of flavocytochrome P450 BM3.
ChainB
Resolution2.0 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) T268 H393 C400
Catalytic site (residue number reindexed from 1) T254 H379 C386
Enzyme Commision number 1.14.14.1: unspecific monooxygenase.
1.6.2.4: NADPH--hemoprotein reductase.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 HEM B K69 L86 W96 A264 G265 T268 T269 F331 P392 H393 R398 C400 I401 G402 A406 K67 L84 W94 A250 G251 T254 T255 F317 P378 H379 R384 C386 I387 G388 A392
Gene Ontology
Molecular Function
GO:0004497 monooxygenase activity
GO:0005506 iron ion binding
GO:0016705 oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
GO:0020037 heme binding

View graph for
Molecular Function
External links
PDB RCSB:1jme, PDBe:1jme, PDBj:1jme
PDBsum1jme
PubMed11695889
UniProtP14779|CPXB_PRIM2 Bifunctional cytochrome P450/NADPH--P450 reductase (Gene Name=cyp102A1)

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