Structure of PDB 4rsn Chain A

Receptor sequence
>4rsnA (length=460) Species: 1404 (Priestia megaterium) [Search protein sequence]
RGSHMTIKEMPQPKTFGELKNLPLLNTDKPVQALMKIADELGEIFKFEAP
GLVTRFLSSQRLIKEACDESRFDKNLSQALKFVRDFAGDGLVTSWTHEKN
WKKAHNILLPSFSQQAMKGYHAMMVDIAVQLVQKWERLNADEHIEVPEDM
TRLTLDTIGLCGFNYRFNSFYRDQPHPFITSMVRALDEAMNKLQRANPDD
PAYDENKRQFQEDIKVMNDLVDKIIADRKASGEQSDDLLTHMLNGKDPET
GEPLDDENIRYQIITFLIAGHVTTSGLLSFALYFLVKNPHVLQKAAEEAA
RVLVDPVPSYKQVKQLKYVDMVLNEALRLWPTAPAFSLYAKEDTVLGGKY
PLEKGDELMVLIPQLHRDKTIWGDDVEEFRPERFENPSAIPQHAFKPFGN
GQRACPGQQFALHEATLVLGMMLKHFDFEDHTNYELDIKETLTLKPEGFV
VKAKSKKIPL
3D structure
PDB4rsn Expanding the drug metabolism function of P450BM3
ChainA
Resolution2.701 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) T273 F398 C405
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 V87 F261 A264 G265 T268 F331 P392 F393 G394 R398 C400 P401 G402 A406 K74 L91 V92 F266 A269 G270 T273 F336 P397 F398 G399 R403 C405 P406 G407 A411
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:4rsn, PDBe:4rsn, PDBj:4rsn
PDBsum4rsn
PubMed
UniProtP14779|CPXB_PRIM2 Bifunctional cytochrome P450/NADPH--P450 reductase (Gene Name=cyp102A1)

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