Structure of PDB 3m4v Chain A

Receptor sequence
>3m4vA (length=451) Species: 1404 (Priestia megaterium) [Search protein sequence]
MPQPKTFGELKNLPLLNTDKPVQALMKIADELGEIFKFEAPGRVTRYLSS
QRLIKEACDESRFDKNLSQALKFVRDFAGDGLFTSWTHEKNWKKAHNILL
PSFSQQAMKGYHAMMVDIAVQLVQKWERLNADEHIEVPEDMTRLTLDTIG
LCGFNYRFNSFYRDQPHPFITSMVRALDEAMNKLQRANPDDPAYDENKRQ
FQEDIKVMNDLVDKIIADRKASGEQSDDLLTHMLNGKDPETGEPLDDENI
RYQIITFLIAGHETTSGLLSFALYFLVKNPHVLQKAAEEAARVLVDPVPS
YKQVKQLKYVGMVLNEALRLWPTAPPFSLYAKEDTVLGGEYPLEKGDELM
VLIPQLHRDKTIWGDDVEEFRPERFENPSAIPQHAFKPFGNGQRACIGQQ
FALHEATLVLGMMLKHFDFEDHTNYELDIKETLTLKPEGFVVKAKSKKIP
L
3D structure
PDB3m4v Structural basis for the properties of two single-site proline mutants of CYP102A1 (P450BM3)
ChainA
Resolution1.9 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 F393 C400
Catalytic site (residue number reindexed from 1) T264 F389 C396
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 A K69 L86 F87 W96 A264 G265 T268 T269 F331 P392 F393 G394 R398 C400 I401 G402 A406 K65 L82 F83 W92 A260 G261 T264 T265 F327 P388 F389 G390 R394 C396 I397 G398 A402
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:3m4v, PDBe:3m4v, PDBj:3m4v
PDBsum3m4v
PubMed21110374
UniProtP14779|CPXB_PRIM2 Bifunctional cytochrome P450/NADPH--P450 reductase (Gene Name=cyp102A1)

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