Structure of PDB 4kpa Chain A

Receptor sequence
>4kpaA (length=461) Species: 1404 (Priestia megaterium) [Search protein sequence]
YFQGAMTIKEMPQPKTFGELKNLPLLNTDKPVQALMKIADELGEIFKFEA
PGRVTRYLSSQRLIKEACDESRFDKNLSQALKFVRDFAGDGLFTSWTHEK
NWKKAHNILLPSFSQQAMKGYHAMMVDIAVQLVQKWERLNADEHIEVPED
MTRLTLDTIGLCGFNYRFNSFYRDQPHPFITSMVRALDEAMNKLQRANPD
DPAYDENKRQFQEDIKVMNDLVDKIIADRKAQSDDLLTHMLNGKDPETGE
PLDDENIRYQIITFLIAGHETTSGLLSFALYFLVKNPHVLQKAAEEAARV
LVDPVPSYKQVKQLKYVGMVLNEALRLWPTAPAFSLYAKEDTVLGGEYPL
EKGDELMVLIPQLHRDKTIWGDDVEEFRPERFENPSAIPQHAFKPFGNGQ
RACIGQQFALHEATLVLGMMLKHFDFEDHTNYELDIKETLTLKPEGFVVK
AKSKKIPLGGI
3D structure
PDB4kpa Structural Evidence: A Single Charged Residue Affects Substrate Binding in Cytochrome P450 BM-3.
ChainA
Resolution2.0 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) T271 F396 C403
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 F107 F261 A264 G265 T268 T269 F331 P392 F393 R398 C400 I401 K75 L92 F93 W102 F113 F264 A267 G268 T271 T272 F334 P395 F396 R401 C403 I404
BS02 140 A R47 Y51 F87 L188 T438 R53 Y57 F93 L194 T441 MOAD: Kd=0.37uM
BindingDB: Kd=82nM
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:4kpa, PDBe:4kpa, PDBj:4kpa
PDBsum4kpa
PubMed23829560
UniProtP14779|CPXB_PRIM2 Bifunctional cytochrome P450/NADPH--P450 reductase (Gene Name=cyp102A1)

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