Structure of PDB 6iao Chain D

Receptor sequence
>6iaoD (length=450) Species: 1404 (Priestia megaterium) [Search protein sequence]
EMPQPKTFGELKNLPLLNTDKPVQALMKIADELGEIFKFEAPGLVTRYLS
SQRLIKEACDGSRFDKNLSQALKFVRDIAGDGLVTSWTHEKNWKKAHNIL
LPSFSQQAMKGYHAMMVDIAVQLVQKWERLNADEHIEVPGDMTRLTLDTI
GLCGFNYRFNSFYRDQPHPFITSMVRALDEAMNKQDDPACDENKRQFQED
IKVMNDLVDKIIADRKASGEQSDDLLTHMLNGKDPETGEPLDDENIRYQI
ITFLIAGHVTTSGLLSFALYFLVKNPYVLQKAAEEAARVLVDPVPSYKQV
KQLKYVGMVLNEALRLWPTAPAFSLYAKEDTVLGGEYPLEKGDELMVLIP
QLHRDKTIWGDDVEEFRPERFENPSAIPQHAFKPFGNGQRACIGQQFALH
EATLVLSMMLKHFDFEDHTNYELDIKETLTLKPEGFVVKAKSKKIPLGGI
3D structure
PDB6iao Structural analysis of Cytochrome P450 BM3 mutant M11 in complex with dithiothreitol.
ChainD
Resolution2.16 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 D K69 L86 V87 W96 F261 A264 G265 T268 F331 P392 F393 R398 C400 I401 A406 K66 L83 V84 W93 F253 A256 G257 T260 F323 P384 F385 R390 C392 I393 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:6iao, PDBe:6iao, PDBj:6iao
PDBsum6iao
PubMed31125381
UniProtP14779|CPXB_PRIM2 Bifunctional cytochrome P450/NADPH--P450 reductase (Gene Name=cyp102A1)

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