Structure of PDB 4o4p Chain B

Receptor sequence
>4o4pB (length=446) Species: 1404 (Priestia megaterium) [Search protein sequence]
EMPQPGELKNLPLLNTDKPVQALMKIADELGEIFKFEAPGRVTRYLSSQR
LIKEACDESRFDKNLSQALKFVRDFFGDGLVTSWTHEKNWKKAHNILLPS
FSQQAMKGYHAMMVDIAVQLVQKWERLNADEHIEVPEDMTRLTLDTIGLC
GFNYRFNSFYRDQPHPFITSMVRALDEAMNKLQRANPDDPAYDENKRQFQ
EDIKVMNDLVDKIIADRKASSDDLLTHMLNGKDPETGEPLDDENIRYQII
TFLIAGHETTSGLLSFALYFLVKNPHVLQKAAEEAARVLVDPVPSYKQVK
QLKYVGMVLNEALRLWPTAPAFSLYAKEDTVLGGEYPLEKGDELMVLIPQ
LHRDKTIWGDDVEEFRPERFENPSAIPQHAFKPFGNGQRACIGQQFALHE
ATLVLGMMLKHFDFEDHTNYELDIKETLTLKPEGFVVKAKSKKIPL
3D structure
PDB4o4p Human P450-like oxidation of diverse proton pump inhibitor drugs by 'gatekeeper' mutants of flavocytochrome P450 BM3.
ChainB
Resolution1.83 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) T259 F384 C391
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 B K69 L86 V87 W96 F261 A264 G265 T268 F331 P392 F393 R398 C400 I401 G402 A406 K63 L80 V81 W90 F252 A255 G256 T259 F322 P383 F384 R389 C391 I392 G393 A397
BS02 1C6 B A74 A264 A328 L437 A68 A255 A319 L428
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:4o4p, PDBe:4o4p, PDBj:4o4p
PDBsum4o4p
PubMed24588219
UniProtP14779|CPXB_PRIM2 Bifunctional cytochrome P450/NADPH--P450 reductase (Gene Name=cyp102A1)

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