Structure of PDB 7yje Chain B

Receptor sequence
>7yjeB (length=454) Species: 1348623 (Priestia megaterium NBRC 15308 = ATCC 14581) [Search protein sequence]
IKEMPQPKTFGELKNLPLLNTDKPVQALMKIADELGEIFKFEAPGRVTRY
LSSQRLIKEACDESRFDKNLSQALKFVRDFAGDGLGTSWTHEKNWKKAHN
ILLPSFSQQAMKGYHAMMVDIAVQLVQKWERLNADEHIEVPEDMTRLTLD
TIGLCGFNYRFNSFYRDQPHPFITSMVRALDEVMNKLQRANPDDPAYDEN
KRQFQEDIKVMNDLVDKIIADRKASGEQSDDLLTHMLNGKDPETGEPLDD
ENIRYQIITFLIAGHEVTSGLLSFALYFLVKNPHVLQKAAEEAARVLVDP
VPSYKQVKQLKYVGMVLNEALRLWPTVPAFSLYAKEDTVLGGEYPLEKGD
ELMVLIPQLHRDKTIWGDDVEEFRPERFENPSAIPQHAFKPFGNGQRACI
GQQFALHEATLVLGMMLKHFDFEDHTNYELDIKETLTLKPEGFVVKAKSK
KIPL
3D structure
PDB7yje Regiodivergent and Enantioselective Hydroxylation of C-H bonds by Synergistic Use of Protein Engineering and Exogenous Dual-Functional Small Molecules.
ChainB
Resolution1.85 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 B K69 L86 G87 W96 F261 A264 V268 T269 V328 F331 P392 F393 G394 R398 C400 I401 G402 K68 L85 G86 W95 F260 A263 V267 T268 V327 F330 P391 F392 G393 R397 C399 I400 G401
BS02 IC6 B P25 Y51 L75 L188 M354 P24 Y50 L74 L187 M353
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:7yje, PDBe:7yje, PDBj:7yje
PDBsum7yje
PubMed36417593
UniProtP14779|CPXB_PRIM2 Bifunctional cytochrome P450/NADPH--P450 reductase (Gene Name=cyp102A1)

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