Structure of PDB 4wg2 Chain A

Receptor sequence
>4wg2A (length=461) Species: 1404 (Priestia megaterium) [Search protein sequence]
EMPQPKTFGELKNLPLLNTDKPVQALMKIADELGEIFKFEAPGRVTRYLS
SQRLIKEACDESRFDKNLSQALKFARDFAGDGLVTSWTHEKNWKKAHNIL
LPSFSQQAMKGYHAMMVDIAVQLVQKWERLNADEHIEVSEDMTRLTLDTI
GLCGFNYRFNSFYRDQPHPFIISMVRALDEVMNKLQRANPDDPAYDENKR
QFQEDIKVMNDLVDKIIADRKARGEQSDDLLTQMLNGKDPETGEPLDDGN
IRYQIITFLFAGHEATSGLLSFALYFLVKNPHVLQKVAEEAARVLVDPVP
SYKQVKQLKYVGMVLNEALRLWPTAPAFSLYAKEDTVLGGEYPLEKGDEV
MVLIPQLHRDKTVWGDDVEEFRPERFENPSAIPQHAFKPFGNGQRASIGQ
QFALHEATLVLGMMLKHFDFEDHTNYELDIKETLSLKPKGFVVKAKSKKI
PLGGIPSPSTH
3D structure
PDB4wg2 Enzyme-controlled nitrogen-atom transfer enables regiodivergent C-h amination.
ChainA
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) A265 F390 S397
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 A K69 L86 V87 W96 G265 A268 T269 F331 P392 F393 G394 R398 S400 G402 A406 K66 L83 V84 W93 G262 A265 T266 F328 P389 F390 G391 R395 S397 G399 A403
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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