Structure of PDB 6alq Chain A Binding Site BS01

Receptor Information
>6alq Chain A (length=337) Species: 1960 (Streptomyces vinaceus) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
RPWSEFRLTPAEAAAAAALAARCAQRYDETDGPEFLLDAPVIAHELPRRL
RTFMARARLDAWPHALVVRGNPVDDAALGSTPVHWRTARTPGSRPLSFLL
MLYAGLLGDVFGWATQQDGRVVTDVLPIKGGEHTLVSSSSRQELGWHTED
AFSPYRADYVGLLSLRNPDGVATTLAGVPLDDLDERTLDVLFQERFLIRP
DDSHLQVNNSTAQQGRVEFEGIAQAADRPEPVAILTGHRAAPHLRVDGDF
SAPAEGDEEAAAALGTLRKLIDASLYELVLDQGDVAFIDNRRAVHGRRAF
QPRYDGRDRWLKRINITRDLHRSRKAWAGDSRVLGQR
Ligand information
Ligand IDFE2
InChIInChI=1S/Fe/q+2
InChIKeyCWYNVVGOOAEACU-UHFFFAOYSA-N
SMILES
SoftwareSMILES
ACDLabs 10.04
OpenEye OEToolkits 1.5.0		[Fe+2]
CACTVS 3.341[Fe++]
FormulaFe
NameFE (II) ION
ChEMBL
DrugBankDB14510
ZINC
PDB chain6alq Chain A Residue 401 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB6alq Visualizing the Reaction Cycle in an Iron(II)- and 2-(Oxo)-glutarate-Dependent Hydroxylase.
Resolution1.67 Å
Binding residue
(original residue number in PDB)		H168 E170 H316
Binding residue
(residue number reindexed from 1)		H147 E149 H295
Annotation score1
Enzymatic activity
Enzyme Commision number 1.14.11.41: L-arginine hydroxylase.
Gene Ontology
Molecular Function
GO:0005506 iron ion binding
GO:0016491 oxidoreductase activity
GO:0016706 2-oxoglutarate-dependent dioxygenase activity
GO:0046872 metal ion binding
GO:0102525 2-oxoglutarate, L-arginine oxygenase (succinate-forming) activity
Biological Process
GO:0017000 antibiotic biosynthetic process
Cellular Component
GO:0016020 membrane

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:6alq, PDBe:6alq, PDBj:6alq
PDBsum6alq
PubMed28823155
UniProtQ6WZB0|ARGHX_STRVI Alpha-ketoglutarate-dependent L-arginine hydroxylase (Gene Name=vioC)

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