Structure of PDB 8hot Chain B

Receptor sequence
>8hotB (length=449) Species: 1404 (Priestia megaterium) [Search protein sequence]
KEMPQPKTFGELKNLPLLNTDKPVQALMKIADELGEIFKFEAPGRVTRYL
SSQRLIKEACDESRFDKNLSQALKFVRDFAGDGLATSWTHEKNWKKAHNI
LLPSFSQQAMKGYHAMMVDIAVQLVQKWERLNADEHIEVPEDMTRLTLDT
IGLCGFNYRFNSFYRDQPHPFITSMVRALDEAMNKLQRPDDPAYDENKRQ
FQEDIKVMNDLVDKIIADRSGEQSDDLLTHMLNGKDPETGEPLDDENIRY
QIITFLIAGHETTSGLLSFALYFLVKNPHVLQKAAEEAARVLVDPVPSYK
QVKQLKYVGMVLNEALRLWPTAPAFSLYAKEDTVLGGEYPLEKGDELMVL
IPQLHRDKTIWGDDVEEFRPERFENPSAIPQHAFKPFGNGQRACIGQQFA
LHEATLVLGMMLKHFDFEDHTNYELDIKETLTLKPEGFVVKAKSKKIPL
3D structure
PDB8hot Crystal structure of the P450 BM3 heme domain mutant F87A in complex with NH2-C7-Phe-Phe
ChainB
Resolution1.96 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 peptide B L20 P25 R47 Y51 S72 Q73 A74 L188 A330 L18 P23 R45 Y49 S70 Q71 A72 L186 A324
BS02 HEM B K69 L86 A87 W96 F107 A264 G265 T268 T269 F331 P392 F393 R398 C400 I401 A406 K67 L84 A85 W94 F105 A258 G259 T262 T263 F325 P386 F387 R392 C394 I395 A400
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:8hot, PDBe:8hot, PDBj:8hot
PDBsum8hot
PubMed
UniProtP14779|CPXB_PRIM2 Bifunctional cytochrome P450/NADPH--P450 reductase (Gene Name=cyp102A1)

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