Structure of PDB 4kpb Chain A

Receptor sequence
>4kpbA (length=440) Species: 1404 (Priestia megaterium) [Search protein sequence]
MPQPKTFGELKNLPLLNTDKPVQALMKIADELGEIFKFEAPGEVTRYLSS
QRLIKEACDESRFDKNLSQALKFVRDFAGDGLFTSWTHEKNWKKAHNILL
PSFSQQAMKGYHAMMVDIAVQLVQKWERLNADEHIEVPEDMTRLTLDTIG
LCGFNYRFNSFYRDQPHPFITSMVRALDEAMNKLDENKRQFQEDIKVMND
LVDKIIADRKASDDLLTHMLNGKDPETGEPLDDENIRYQIITFLIAGHET
TSGLLSFALYFLVKNPHVLQKAAEEAARVLVDPVPSYKQVKQLKYVGMVL
NEALRLWPTAPAFSLYAKEDTVLGGEYPLEKGDELMVLIPQLHRDKTIWG
DDVEEFRPERFENPSAIPQHAFKPFGNGQRACIGQQFALHEATLVLGMML
KHFDFEDHTNYELDIKETLTLKPEGFVVKAKSKKIPLGGI
3D structure
PDB4kpb Structural Evidence: A Single Charged Residue Affects Substrate Binding in Cytochrome P450 BM-3.
ChainA
Resolution2.1 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) T250 F375 C382
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 R398 C400 I401 G402 A406 K65 L82 F83 W92 A246 G247 T250 T251 F313 P374 F375 R380 C382 I383 G384 A388
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:4kpb, PDBe:4kpb, PDBj:4kpb
PDBsum4kpb
PubMed23829560
UniProtP14779|CPXB_PRIM2 Bifunctional cytochrome P450/NADPH--P450 reductase (Gene Name=cyp102A1)

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