Structure of PDB 6jvc Chain A

Receptor sequence
>6jvcA (length=454) Species: 1404 (Priestia megaterium) [Search protein sequence]
IKEMPQPKTFGELKNLPLLNTDKPVQALMKIADELGEIFKFEAPGRVTRY
LSSQRLIKEACDESRFDKNLSQALKFVRDFAGDGLFTSWTHEKNWKKAHN
ILLPSFSQQAMKGYHAMMVDIAVQLVQKWERLNADEHIEVPEDMTRLTLD
TIGLCGFNYRFNSFYRDQPHPFITSMVRALDEAMNKLQRANPDDPAYDEN
KRQFQEDIKVMNDLVDKIIADRKASGEQSDDLLTHMLNGKDPETGEPLDD
ENIRYQIITFLIAGHETTSGLLSFALYFLVKNPHVLQKAAEEAARVLVDP
VPSYKQVKQLKYVGMVLNEALRLWPTAPAFSLYAKEDTVLGGEYPLEKGD
ELMVLIPQLHRDKTIWGDDVEEFRPERFENPSAIPQHAFKPFGNGQRACI
GQQFALHEATLVLGMMLKHFDFEDHTNYELDIKETLTLKPEGFVVKAKSK
KIPL
3D structure
PDB6jvc Crystals in Minutes: Instant On-Site Microcrystallisation of Various Flavours of the CYP102A1 (P450BM3) Haem Domain.
ChainA
Resolution1.75 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) T267 F392 C399
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 WAA A R47 Y51 S72 Q73 A74 F87 L437 R46 Y50 S71 Q72 A73 F86 L436
BS02 COH A K69 L86 F87 W96 A264 G265 T268 T269 F331 P392 F393 R398 C400 I401 G402 K68 L85 F86 W95 A263 G264 T267 T268 F330 P391 F392 R397 C399 I400 G401
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:6jvc, PDBe:6jvc, PDBj:6jvc
PDBsum6jvc
PubMed32157795
UniProtP14779|CPXB_PRIM2 Bifunctional cytochrome P450/NADPH--P450 reductase (Gene Name=cyp102A1)

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