Structure of PDB 4h23 Chain A

Receptor sequence
>4h23A (length=454) Species: 1404 (Priestia megaterium) [Search protein sequence]
IKEMPQPKTFGELKNLPLLNTDKPVQALMKIADELGEIFKFEAPGRVTRY
LSSQRLIKEACDESRFDKNLSQALKFARDFAGDGLVTSWTHEKNWKKAHN
ILLPSFSQQAMKGYHAMMVDIAVQLVQKWERLNADEHIEVSEDMTRLTLD
TIGLCGFNYRFNSFYRDQPHPFIISMVRALDEVMNKLQRANPDDPAYDEN
KRQFQEDIKVMNDLVDKIIADRKARGEQSDDLLTQMLNGKDPETGEPLDD
GNIRYQIITFLIAGHEATSGLLSFALYFLVKNPHVLQKVAEEAARVLVDP
VPSYKQVKQLKYVGMVLNEALRLWPTAPAFSLYAKEDTVLGGEYPLEKGD
EVMVLIPQLHRDKTVWGDDVEEFRPERFENPSAIPQHAFKPFGNGQRASI
GQQFALHEATLVLGMMLKHFDFEDHTNYELDIKETLTLKPKGFVVKAKSK
KIPL
3D structure
PDB4h23 A serine-substituted P450 catalyzes highly efficient carbene transfer to olefins in vivo.
ChainA
Resolution3.3 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) A267 F392 S399
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 W96 F107 F261 G265 A268 A328 F331 P392 F393 R398 S400 I401 G402 A406 K68 L85 W95 F106 F260 G264 A267 A327 F330 P391 F392 R397 S399 I400 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:4h23, PDBe:4h23, PDBj:4h23
PDBsum4h23
PubMed23792734
UniProtP14779|CPXB_PRIM2 Bifunctional cytochrome P450/NADPH--P450 reductase (Gene Name=cyp102A1)

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