Structure of PDB 7wg0 Chain A

Receptor sequence
>7wg0A (length=454) Species: 1404 (Priestia megaterium) [Search protein sequence]
IKEMPQPKTFGELKNLPLLNTDKPVQALMKIADELGEIFKFEAPGRVTRY
LSSQRLIKEACDESRFDKNLSQALKFVRDFAGDGLFTSWTHEKNWKKAHN
ILLPSFSQQAMKGYHAMMVDIAVQLVQKWERLNADEHIEVPEDMTRLTLD
TIGLCGFNYRFNSFYRDQPHPFITSMVRALDEAMNKLQRANPDDPAYDEN
KRQFQEDIKVMNDLVDKIIADRKASGEQSDDLLTHMLNGKDPETGEPLDD
ENIRYQIITFLIAGHETTSGLLSFALYFLVKNPHVLQKAAEEAARVLVDP
VPSYKQVKQLKYVGMVLNEALRLWPTAPAFSLYAKEDTVLGGEYPLEKGD
ELMVLIPQLHRDKTIWGDDVEEFRPERFENPSAIPQHAFKPFGNGQRACP
GQQFALHEATLVLGMMLKHFDFEDHTNYELDIKETLTLKPEGFVVKAKSK
KIPL
3D structure
PDB7wg0 Structure of the Manganese Protoporphyrin IX-Reconstituted CYP102A1 Heme Domain with N-palmitoyl-L-phenylalanine
ChainA
Resolution2.2 Å
3D
structure
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Enzymatic activity
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 XPZ A R47 Y51 S72 Q73 A74 L188 T260 A330 R46 Y50 S71 Q72 A73 L187 T259 A329
BS02 MNH A K69 L86 F87 W96 F261 A264 G265 T268 T269 F331 P392 F393 R398 C400 P401 G402 A406 K68 L85 F86 W95 F260 A263 G264 T267 T268 F330 P391 F392 R397 C399 P400 G401 A405
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:7wg0, PDBe:7wg0, PDBj:7wg0
PDBsum7wg0
PubMed
UniProtP14779|CPXB_PRIM2 Bifunctional cytochrome P450/NADPH--P450 reductase (Gene Name=cyp102A1)

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