Structure of PDB 8hos Chain A Binding Site BS01
Receptor Information
>8hos Chain A (length=446) Species:
1404
(Priestia megaterium) [
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KEMPQPKTFGELKNLPLLNTDKPVQALMKIADELGEIFKFEAPGRVTRYL
SSQRLIKEACDESRFDKNLSQALKFVRDFAGDGLATSWTHEKNWKKAHNI
LLPSFSQQAMKGYHAMMVDIAVQLVQKWERLNADEHIEVPEDMTRLTLDT
IGLCGFNYRFNSFYRDQPHPFITSMVRALDEAMNKLQRYDENKRQFQEDI
KVMNDLVDKIIADRKASGEQSDDLLTHMLNGKDPETGEPLDDENIRYQII
TFLIAGHETTSGLLSFALYFLVKNPHVLQKAAEEAARVLVDPVPSYKQVK
QLKYVGMVLNEALRLWPTAPAFSLYAKEDTVLGGEYPLEKGDELMVLIPQ
LHRDKTIWGDDVEEFRPERFENPSAIPQHAFKPFGNGQRACIGQQFALHE
ATLVLGMMLKHFDFEDHTNYELDIKETLTLKPEGFVVKAKSKKIPL
Ligand information
>8hos Chain C (length=2) Species:
32630
(synthetic construct) [
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FY
Receptor-Ligand Complex Structure
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PDB
8hos
Crystal structure of the P450 BM3 heme domain mutant F87A in complex with Im-C6-Phe(4NO2)-Tyr
Resolution
1.82 Å
Binding residue
(original residue number in PDB)
L20 P25 F42 R47 Y51 S72 Q73 A74 M185 L188 Q189 A328 A330 M354 L437
Binding residue
(residue number reindexed from 1)
L18 P23 F40 R45 Y49 S70 Q71 A72 M183 L186 Q187 A319 A321 M345 L428
Enzymatic activity
Enzyme Commision number
1.14.14.1
: unspecific monooxygenase.
1.6.2.4
: NADPH--hemoprotein reductase.
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:8hos
,
PDBe:8hos
,
PDBj:8hos
PDBsum
8hos
PubMed
37713467
UniProt
P14779
|CPXB_PRIM2 Bifunctional cytochrome P450/NADPH--P450 reductase (Gene Name=cyp102A1)
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