Structure of PDB 4wg2 Chain B

Receptor sequence
>4wg2B (length=451) Species: 1404 (Priestia megaterium) [Search protein sequence]
KEMPQPKTFGELKNLPLLNTDKPVQALMKIADELGEIFKFEAPGRVTRYL
SSQRLIKEACDESRFDKNLSQALKFARDFAGDGLVTSWTHEKNWKKAHNI
LLPSFSQQAMKGYHAMMVDIAVQLVQKWERLNADEHIEVSEDMTRLTLDT
IGLCGFNYRFNSFYRDQPHPFIISMVRALDEVMNKLQRANPAYDENKRQF
QEDIKVMNDLVDKIIADRKAEQSDDLLTQMLNGKDPETGEPLDDGNIRYQ
IITFLFAGHEATSGLLSFALYFLVKNPHVLQKVAEEAARVLVDPVPSYKQ
VKQLKYVGMVLNEALRLWPTAPAFSLYAKEDTVLGGEYPLEKGDEVMVLI
PQLHRDKTVWGDDVEEFRPERFENPSAIPQHAFKPFGNGQRASIGQQFAL
HEATLVLGMMLKHFDFEDHTNYELDIKETLSLKPKGFVVKAKSKKIPLGG
I
3D structure
PDB4wg2 Enzyme-controlled nitrogen-atom transfer enables regiodivergent C-h amination.
ChainB
Resolution2.66 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) A268 F393 S400
Catalytic site (residue number reindexed from 1) A261 F386 S393
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 G265 A268 T269 A328 F331 P392 F393 R398 S400 G402 A406 K67 L84 V85 G258 A261 T262 A321 F324 P385 F386 R391 S393 G395 A399
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:4wg2, PDBe:4wg2, PDBj:4wg2
PDBsum4wg2
PubMed25325618
UniProtP14779|CPXB_PRIM2 Bifunctional cytochrome P450/NADPH--P450 reductase (Gene Name=cyp102A1)

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