Structure of PDB 5og9 Chain A

Receptor sequence
>5og9A (length=454) Species: 1404 (Priestia megaterium) [Search protein sequence]
KEMPQPKTFGELKNLPLLNTDKPVQALMKIADELGEIFKFEAPGWVTRWL
SSQRLIKEACDESRFDKNLIQALKFVRDFFGDGLITSWTHEKNWKKAHNI
LLPSFSQQAMKGYHAMMVDIAVQLVQKWERLNADEHIEVPEDMTRLTLDT
IGLCGFNYRFNSFYRDQPHPFITSMVRACDEAMNKLQRNPDDPAYDENKR
QFQEDIKVMNDLVDKIIADRKASGEQSDDLLTHMLNGKDPETGEPLDDEN
IRYQIITFLIAGHETTSGLLSFALYFLVKNPHVLQKAAEEAARVLVDPVP
SYKQVKQLKYVGMVLNEALRLWPTAPAFSLYAKEDTVLGGEYPLEKGDEL
MVLIPQLHRDKTIWGDDVEEFRPERFENPSAIPQHAFKPFGNGQRACIGQ
QFALHEATLVLGMMLKHFDFEDHTNYELDIKETLTLKPEGFVVKAKSKKI
PLGG
3D structure
PDB5og9 Regio- and diastereoselective hydroxylation of steroids using P450-BM3: Readdressing the numbers problem in directed evolution
ChainA
Resolution2.09 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 HEM A K70 L87 I88 W97 F262 A265 G266 T269 F332 P393 F394 R399 C401 I402 G403 A407 K67 L84 I85 W94 F258 A261 G262 T265 F328 P389 F390 R395 C397 I398 G399 A403
BS02 ZN A H139 E141 H136 E138
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:5og9, PDBe:5og9, PDBj:5og9
PDBsum5og9
PubMed
UniProtP14779|CPXB_PRIM2 Bifunctional cytochrome P450/NADPH--P450 reductase (Gene Name=cyp102A1)

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