Structure of PDB 6dax Chain A Binding Site BS03

Receptor Information

>6dax Chain A (length=338) Species: 1960 (Streptomyces vinaceus)

VRPWSEFRLTPAEAAAAAALAARCAQRYDETDGPEFLLDAPVIAHELPRR
LRTFMARARLDAWPHALVVRGNPVDDAALGSTPVHWRTARTPGSRPLSFL
LMLYAGLLGDVFGWATQQDGRVVTDVLPIKGGEHTLVSSSSRQELGWHTE
DAFSPYRADYVGLLSLRNPDGVATTLAGVPLDDLDERTLDVLFQERFLIR
PDDSHLQVNNSTAQQGRVEFEGIAQAADRPEPVAILTGHRAAPHLRVDGD
FSAPAEGDEEAAAALGTLRKLIDASLYELVLDQGDVAFIDNRRAVHGRRA
FQPRYDGRDRWLKRINITRDLHRSRKAWAGDSRVLGQR

Ligand information

• Ligand ID: FE2
• InChI: InChI=1S/Fe/q+2
• InChIKey: CWYNVVGOOAEACU-UHFFFAOYSA-N
• SMILES:
  ACDLabs 10.04
  OpenEye OEToolkits 1.5.0: [Fe+2]
  CACTVS 3.341: [Fe++]
• Formula: Fe
• Name: FE (II) ION
• DrugBank: DB14510
• PDB chain: 6dax Chain A Residue 403

Receptor-Ligand Complex Structure

Structure summary

• PDB: 6dax Two Distinct Mechanisms for C-C Desaturation by Iron(II)- and 2-(Oxo)glutarate-Dependent Oxygenases: Importance of alpha-Heteroatom Assistance.
• Resolution: 1.7 Å
• Binding residue (original residue number in PDB): H168 E170 H316
• Binding residue (residue number reindexed from 1): H148 E150 H296
• Annotation score: 1

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

External links

• PDB: RCSB:6dax, PDBe:6dax, PDBj:6dax
• PDBsum: 6dax
• PubMed: 29708749
• UniProt: Q6WZB0|ARGHX_STRVI Alpha-ketoglutarate-dependent L-arginine hydroxylase (Gene Name=vioC)