Structure of PDB 8hoq Chain B

Receptor sequence
>8hoqB (length=450) Species: 1404 (Priestia megaterium) [Search protein sequence]
KEMPQPKTFGELKNLPLLNTDKPVQALMKIADELGEIFKFEAPGRVTRYL
SSQRLIKEACDESRFDKNLSQALKFVRDFAGDGLATSWTHEKNWKKAHNI
LLPSFSQQAMKGYHAMMVDIAVQLVQKWERLNADEHIEVPEDMTRLTLDT
IGLCGFNYRFNSFYRDQPHPFITSMVRALDEAMNKLQRDDPAYDENKRQF
QEDIKVMNDLVDKIIADRKASGEQSDDLLTHMLNGKDPETGEPLDDENIR
YQIITFLIAGHETTSGLLSFALYFLVKNPHVLQKAAEEAARVLVDPVPSY
KQVKQLKYVGMVLNEALRLWPTAPAFSLYAKEDTVLGGEYPLEKGDELMV
LIPQLHRDKTIWGDDVEEFRPERFENPSAIPQHAFKPFGNGQRACIGQQF
ALHEATLVLGMMLKHFDFEDHTNYELDIKETLTLKPEGFVVKAKSKKIPL
3D structure
PDB8hoq Crystal structure of the P450 BM3 heme domain mutant F87A in complex with Im-C6-Phe(4CF3)-Tyr
ChainB
Resolution1.94 Å
3D
structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
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 F42 R47 Y51 S72 Q73 A74 M185 L188 Q189 M354 L18 P23 F40 R45 Y49 S70 Q71 A72 M183 L186 Q187 M349
BS02 HEM B K69 L86 A87 W96 A264 G265 T268 F331 P392 F393 R398 C400 I401 G402 A406 K67 L84 A85 W94 A259 G260 T263 F326 P387 F388 R393 C395 I396 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:8hoq, PDBe:8hoq, PDBj:8hoq
PDBsum8hoq
PubMed37713467
UniProtP14779|CPXB_PRIM2 Bifunctional cytochrome P450/NADPH--P450 reductase (Gene Name=cyp102A1)

[Back to BioLiP]