Structure of PDB 6k9s Chain B

Receptor sequence
>6k9sB (length=449) Species: 1404 (Priestia megaterium) [Search protein sequence]
TIKEMPQPKTFGELKNLPLLNTDKPVQALMKIADELGEIFKFEAPGRVTR
YLSSQRLIKEACDESRFDKNLSQALKFVRDFAGDGLFTSWTHEKNWKKAH
NILLPSFSQQAMKGYHAMMVDIAVQLVQKWERLNADEHIEVPEDMTRLTL
DTIGLCGFNYRFNSFYRDQPHPFITSMVRALDEAMNKLQRANPDDPAYDE
NKRQFQEDIKVMNDLVDKIIADRSDDLLTHMLNGKDPETGEPLDDENIRY
QIITFLIAGHETTSGLLSFALYFLVKNPHVLQKAAEEAARVLVDPVPSYK
QVKQLKYVGMVLNEALRLWPTAPAFSLYAKEDTVLGGEYPLEKGDELMVL
IPQLHRDKTIWGDDVEEFRPERFENPSAIPQHAFKPFGNGQRACIGQQFA
LHEATLVLGMMLKHFDFEDHTNYELDIKETLTLKPEGFVVKAKSKKIPL
3D structure
PDB6k9s Crystals in Minutes: Instant On-Site Microcrystallisation of Various Flavours of the CYP102A1 (P450BM3) Haem Domain.
ChainB
Resolution1.55 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) T262 F387 C394
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 RUR B K69 L86 F87 W96 F107 A264 G265 T268 F331 P392 F393 R398 C400 I401 G402 A406 K69 L86 F87 W96 F107 A258 G259 T262 F325 P386 F387 R392 C394 I395 G396 A400
BS02 WAA B L20 R47 Y51 S72 Q73 A74 L188 A328 A330 M354 L437 L20 R47 Y51 S72 Q73 A74 L188 A322 A324 M348 L431
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:6k9s, PDBe:6k9s, PDBj:6k9s
PDBsum6k9s
PubMed32157795
UniProtP14779|CPXB_PRIM2 Bifunctional cytochrome P450/NADPH--P450 reductase (Gene Name=cyp102A1)

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