Structure of PDB 6ly4 Chain A

Receptor sequence
>6ly4A (length=450) Species: 1348623 (Priestia megaterium NBRC 15308 = ATCC 14581) [Search protein sequence]
KEMPQPKTFGELKNLPLLNTDKPVQALMKIADELGEIFKFEAPGWVTRYL
SSQRLIKEACDESRFDKNLWQALKYLRDILGDGLGSSWTHEKNWKKAHNI
LLPSFSQQAMKGYHAMMVDIAVQLVQKWERLNADEHIEVPEDMTRLTLDT
IGLCGFNYRFNSFYRDQPHPFITSTVRALDEAQNKQQRANPDDPAYDENK
RQFQEDTKVMNDLVDKIIADRKASSDDLLTHMLNGKDPETGEPLDDENIR
YQIITFLIAGHETTSGLLSFALYFLVKNPHVLQKAAEEAARVLVDPVPSY
KQVKQLKYVGMVLNEALRLWPTGPWFSLYAKEDTVLGGEYPLEKGDELMV
LIPQLHRDKTIWGDDVEEFRPERFENPSAIPQHAFKPFGNGQRACIGQQF
ALHEATLVLGMMLKHFDFEDHTNYELDIKETLTLKPEGFVVKAKSKKIPL
3D structure
PDB6ly4 Regio- and Stereoselective Steroid Hydroxylation at C7 by Cytochrome P450 Monooxygenase Mutants.
ChainA
Resolution1.68 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 TES A L82 G87 T260 G328 P329 L437 L80 G85 T255 G323 P324 L432
BS02 HEM A K69 L86 W96 F261 A264 G265 T268 F331 P392 F393 R398 C400 I401 G402 A406 K67 L84 W94 F256 A259 G260 T263 F326 P387 F388 R393 C395 I396 G397 A401
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:6ly4, PDBe:6ly4, PDBj:6ly4
PDBsum6ly4
PubMed32243054
UniProtP14779|CPXB_PRIM2 Bifunctional cytochrome P450/NADPH--P450 reductase (Gene Name=cyp102A1)

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