BioLiP

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

PDB

7wg0 Structure of the Manganese Protoporphyrin IX-Reconstituted CYP102A1 Heme Domain with N-palmitoyl-L-phenylalanine

Chain

Resolution

2.2 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

PDB	RCSB:7wg0, PDBe:7wg0, PDBj:7wg0
PDBsum	7wg0
PubMed
UniProt	P14779\|CPXB_PRIM2 Bifunctional cytochrome P450/NADPH--P450 reductase (Gene Name=cyp102A1)