Structure of PDB 6daz Chain A Binding Site BS01

Receptor Information
>6daz Chain A (length=336) Species: 1960 (Streptomyces vinaceus) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
PWSEFRLTPAEAAAAAALAARCAQRYDETDGPEFLLDAPVIAHELPRRLR
TFMARARLDAWPHALVVRGNPVDDAALGSTPVHWRTARTPGSRPLSFLLM
LYAGLLGDVFGWATQQDGRVVTDVLPIKGGEHTLVSSSSRQELGWHTEDA
FSPYRADYVGLLSLRNPDGVATTLAGVPLDDLDERTLDVLFQERFLIRPD
DSHLQVNNSTAQQGRVEFEGIAQAADRPEPVAILTGHRAAPHLRVDGDFS
APAEGDEEAAAALGTLRKLIDASLYELVLDQGDVAFIDNRRAVHGRRAFQ
PRYDGRDRWLKRINITRDLHRSRKAWAGDSRVLGQR
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 chain6daz 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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PDB6daz Two Distinct Mechanisms for C-C Desaturation by Iron(II)- and 2-(Oxo)glutarate-Dependent Oxygenases: Importance of alpha-Heteroatom Assistance.
Resolution1.94 Å
Binding residue
(original residue number in PDB)		H168 E170 H316
Binding residue
(residue number reindexed from 1)		H146 E148 H294
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:6daz, PDBe:6daz, PDBj:6daz
PDBsum6daz
PubMed29708749
UniProtQ6WZB0|ARGHX_STRVI Alpha-ketoglutarate-dependent L-arginine hydroxylase (Gene Name=vioC)

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