Structure of PDB 6db2 Chain A Binding Site BS02

Receptor Information

>6db2 Chain A (length=336) Species: 1960 (Streptomyces vinaceus)

PWSEFRLTPAEAAAAAALAARCAQRYDETDGPEFLLDAPVIAHELPRRLR
TFMARARLDAWPHALVVRGNPVDDAALGSTPVHWRTARTPGSRPLSFLLM
LYAGLLGDVFGWATQQDGRVVTDVLPIKGGEHTLVSSSSRQELGWHTEDA
FSPYRADYVGLLSLRNPDGVATTLAGVPLDDLDERTLDVLFQERFLIRPD
DSHLQVNNSTAQQGRVEFEGIAQAADRPEPVAILTGHRAAPHLRVDGDFS
APAEGDEEAAAALGTLRKLIDASLYELVLDQGDVAFIDNRRAVHGRRAFQ
PRYDGRDRWLKRINITRDLHRSRKAWAGDSRVLGQR

Ligand information

• Ligand ID: VVO
• InChI: InChI=1S/O.V/q;+2
• InChIKey: MHHDXUNFNAZUGB-UHFFFAOYSA-N
• SMILES:
  ACDLabs 12.01
  OpenEye OEToolkits 2.0.6: O=[V+2]
  CACTVS 3.385: O=[V++]
• Formula: O V
• Name: oxovanadium(2+)
• PDB chain: 6db2 Chain A Residue 403

Receptor-Ligand Complex Structure

Structure summary

• PDB: 6db2 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): H146 E148 H294
• 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:6db2, PDBe:6db2, PDBj:6db2
• PDBsum: 6db2
• PubMed: 29708749
• UniProt: Q6WZB0|ARGHX_STRVI Alpha-ketoglutarate-dependent L-arginine hydroxylase (Gene Name=vioC)