Structure of PDB 4h24 Chain B

Receptor sequence
>4h24B (length=452) Species: 1404 (Priestia megaterium) [Search protein sequence]
TIKEMPQPKTFGELKNLPLLNTDKPVQALMKIADELGEIFKFEAPGRVTR
YLSSQRLIKEACDESRFDKNLSQALKFARDFAGDGLVTSWTHEKNWKKAH
NILLPSFSQQAMKGYHAMMVDIAVQLVQKWERLNADEHIEVSEDMTRLTL
DTIGLCGFNYRFNSFYRDQPHPFIISMVRALDEVMNKLQRANPDDPAYDE
NKRQFQEDIKVMNDLVDKIIADRKADDLLTQMLNGKDPETGEPLDDGNIR
YQIITFLIAGHEATSGLLSFALYFLVKNPHVLQKVAEEAARVLVDPVPSY
KQVKQLKYVGMVLNEALRLWPTAPAFSLYAKEDTVLGGEYPLEKGDEVMV
LIPQLHRDKTVWGDDVEEFRPERFENPSAIPQHAFKPFGNGQRACIGQQF
ALHEATLVLGMMLKHFDFEDHTNYELDIKETLTLKPKGFVVKAKSKKIPL
GG
3D structure
PDB4h24 A serine-substituted P450 catalyzes highly efficient carbene transfer to olefins in vivo.
ChainB
Resolution2.5 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 C400
Catalytic site (residue number reindexed from 1) A263 F388 C395
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 W96 F107 F261 G265 A268 T269 F331 P392 F393 R398 C400 G402 A406 K69 L86 V87 W96 F107 F256 G260 A263 T264 F326 P387 F388 R393 C395 G397 A401
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:4h24, PDBe:4h24, PDBj:4h24
PDBsum4h24
PubMed23792734
UniProtP14779|CPXB_PRIM2 Bifunctional cytochrome P450/NADPH--P450 reductase (Gene Name=cyp102A1)

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