Structure of PDB 6h1l Chain A

Receptor sequence
>6h1lA (length=451) Species: 1404 (Priestia megaterium) [Search protein sequence]
KEMPQPKTFGELKNLPLLNTDKPVQALMKIADELGEIFKFEAPGRVTRYL
SSQRLIKEACDESRFDKNLSQALKFVRDFFGDGLVTSWTHEKNWKKAHNI
LLPSFSQQAMKGYHAMMVDIAVQLVQKWERLNADEHIEVPEDMTRLTLDT
IGLCGFNYRFNSFYRDQPHPFITSMVRALDEAMNKLQDDPAYDENKRQFQ
EDIKVMNDLVDKIIADRKASGEQSDDLLTHMLNGKDPETGEPLDDENIRY
QIITFLIAGHETTSGLLSFALYFLVKNPHVLQKAAEEAARVLVDPVPSYK
QVKQLKYVGMVLNEALRLWPTAPAFSLYAKEDTVLGGEYPLEKGDELMVL
IPQLHRDKTIWGDDVEEFRPERFENPSAIPQHAFKPFGNGQRACIGQQFA
LHEATLVLGMMLKHFDFEDHTNYELDIKETLTLKPEGFVVKAKSKKIPLG
G
3D structure
PDB6h1l Novel insights into P450 BM3 interactions with FDA-approved antifungal azole drugs.
ChainA
Resolution1.968 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) T268 F393 C400
Catalytic site (residue number reindexed from 1) T262 F387 C394
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 FJQ A L75 F82 V87 A264 T268 L437 L73 F80 V85 A258 T262 L431 MOAD: Kd=24.5uM
BS02 HEM A K69 L86 V87 W96 F261 A264 G265 T268 F331 P392 F393 G394 R398 C400 I401 G402 A406 K67 L84 V85 W94 F255 A258 G259 T262 F325 P386 F387 G388 R392 C394 I395 G396 A400
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:6h1l, PDBe:6h1l, PDBj:6h1l
PDBsum6h1l
PubMed30733479
UniProtF2Q7T0

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