Structure of PDB 5og9 Chain B

Receptor sequence
>5og9B (length=454) Species: 1404 (Priestia megaterium) [Search protein sequence]
KEMPQPKTFGELKNLPLLNTDKPVQALMKIADELGEIFKFEAPGWVTRWL
SSQRLIKEACDESRFDKNLIQALKFVRDFFGDGLITSWTHEKNWKKAHNI
LLPSFSQQAMKGYHAMMVDIAVQLVQKWERLNADEHIEVPEDMTRLTLDT
IGLCGFNYRFNSFYRDQPHPFITSMVRACDEAMNKLQRANPDDPAYDENK
RQFQEDIKVMNDLVDKIIADRKASGEQSDDLLTHMLNGKDPETGEPLDDE
NIRYQIITFLIAGHETTSGLLSFALYFLVKNPHVLQKAAEEAARVLVDPV
PSYKQVKQLKYVGMVLNEALRLWPTAPAFSLYAKEDTVLGGEYPLEKGDE
LMVLIPQLHRDKTIWGDDVEEFRPERFENPSAIPQHAFKPFGNGQRACIG
QQFALHEATLVLGMMLKHFDFEDHTNYELDIKETLTLKPEGFVVKAKSKK
IPLG
3D structure
PDB5og9 Regio- and diastereoselective hydroxylation of steroids using P450-BM3: Readdressing the numbers problem in directed evolution
ChainB
Resolution2.09 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 ZN B D339 E349 D336 E346
BS02 HEM B K70 L87 I88 W97 F262 A265 G266 T269 F332 P393 F394 R399 C401 I402 G403 A407 K67 L84 I85 W94 F259 A262 G263 T266 F329 P390 F391 R396 C398 I399 G400 A404
BS03 TES B L21 M186 L189 L438 L18 M183 L186 L435
BS04 TES B L72 I73 V79 I88 A329 L69 I70 V76 I85 A326
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)

[Back to BioLiP]