Structure of PDB 5e78 Chain A

Receptor sequence
>5e78A (length=447) Species: 1404 (Priestia megaterium) [Search protein sequence]
KEMPQPKTFGELKNLPLLNTDKPVQALMKIADELGEIFKFEAPGRVTRYL
SSQRLIKEACDESRFDKNLSQALKFVRDFAGDGLATSWTHEKNWKKAHNI
LLPSFSQQAMKGYHAMMVDIAVQLVQKWERLNADEHIEVPEDMTRLTLDT
IGLCGFNYRFNSFYRDQPHPFITSMVRALDEAMNKLQRAYDENKRQFQED
IKVMNDLVDKIIADRKASGEQSDDLLTHMLNGKDPETGEPLDDENIRYQI
ITFLIAGHETTSGLLSFALYFLGKNPHVLQKAAEEAARVLVDPVPSYKQV
KQLKYVGMVLNEALRLWPTAPAFSLYAKEDTVLGGEYPLEKGDELSVLIP
QLHRDKTIWGDDVEEFRPERFENPSAIPQHAFKPFGNGQRACIGQQFALH
EATLVLGMMLKHFDFEDHTNYELDIKETLTLKPEGFVVKAKSKKIPL
3D structure
PDB5e78 Crystallographic insights into a cobalt (III) sepulchrate based alternative cofactor system of P450 BM3 monooxygenase.
ChainA
Resolution2.0 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) T268 F393 C400
Catalytic site (residue number reindexed from 1) T260 F385 C392
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 A87 W96 A264 G265 T268 F331 P392 F393 R398 C400 I401 G402 A406 K67 L84 A85 W94 A256 G257 T260 F323 P384 F385 R390 C392 I393 G394 A398
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:5e78, PDBe:5e78, PDBj:5e78
PDBsum5e78
PubMed28739446
UniProtP14779|CPXB_PRIM2 Bifunctional cytochrome P450/NADPH--P450 reductase (Gene Name=cyp102A1)

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