Structure of PDB 1zoa Chain B

Receptor sequence
>1zoaB (length=457) Species: 1404 (Priestia megaterium) [Search protein sequence]
IKEMPQPKTFGELKNLPLLNTDKPVQALMKIADELGEIFKFEAPGRVTRY
LSSQRLIKEACDESRFDKNLSQALKFVRDFAGDGLFTSWTHEKNWKKAHN
ILLPSFSQQAMKGYHAMMVDIAVQLVQKWERLNADEHIEVPEDMTRLTLD
TIGLCGFNYRFNSFYRDQPHPFITSMVRALDEAMNKLQRANPDDPAYDEN
KRQFQEDIKVMNDLVDKIIADRKASGEQSDDLLTHMLNGKDPETGEPLDD
ENIRYQIITFLIAGHETTSGLLSFALYFLVKNPHVLQKAAEEAARVLVDP
VPSYKQVKQLKYVGMVLNEALRLWPTVPAFSLYAKEDTVLGGEYPLEKGD
ELMVLIPQLHRDKTIWGDDVEEFRPERFENPSAIPQHAFKPFGNGQRACI
GQQFALHEATLVLGMMLKHFDFEDHTNYELDIKETLTLKPEGFVVKAKSK
KIPLGGI
3D structure
PDB1zoa A single active-site mutation of P450BM-3 dramatically enhances substrate binding and rate of product formation.
ChainB
Resolution1.74 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) T267 F392 C399
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 F87 W96 F107 F261 A264 G265 T268 V328 F331 P392 F393 R398 C400 I401 A406 K68 L85 F86 W95 F106 F260 A263 G264 T267 V327 F330 P391 F392 R397 C399 I400 A405
BS02 140 B Y51 S72 Q73 A74 F87 Y50 S71 Q72 A73 F86 MOAD: Kd=45nM
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:1zoa, PDBe:1zoa, PDBj:1zoa
PDBsum1zoa
PubMed21875028
UniProtP14779|CPXB_PRIM2 Bifunctional cytochrome P450/NADPH--P450 reductase (Gene Name=cyp102A1)

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