› 9eqf

X-ray diffraction
1.6Å resolution

Crystal structure of the L-arginine hydroxylase VioC MeHis316, bound to Fe(II), L-arginine, and succinate

Released:
DOI: 10.2210/pdb9eqf/pdb
PDB entry 9eqf coloured by chain, front view.
PDB entry 9eqf coloured by chain, side view.
PDB entry 9eqf coloured by chain, top view.
Source organism: synthetic construct
Primary publication:
Probing Ferryl Reactivity in a Nonheme Iron Oxygenase Using an Expanded Genetic Code.
Hardy FJ, Quesne MG, Gérard EF, Zhao J, Ortmayer M, Taylor CJ, Ali HS, Slater JW, Levy CW, Heyes DJ, Bollinger JM, de Visser SP, Green AP
ACS Catal 14 11584-11590 (2024)
PMID: 39114090

Function and Biology Details

Reaction catalysed: 
L-arginine + 2-oxoglutarate + O(2) = (3S)-3-hydroxy-L-arginine + succinate + CO(2)
Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-180511 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Alpha-ketoglutarate-dependent L-arginine hydroxylase Chain: A
Molecule details ›
Chain: A
Length: 394 amino acids
Theoretical weight: 43.32 KDa
Source organism: synthetic construct
Expression system: Escherichia coli
UniProt:
  • Canonical: Q6WZB0 (Residues: 1-358; Coverage: 100%)
Gene name: vioC
Sequence domains: Taurine catabolism dioxygenase TauD, TfdA family

Ligands and Environments

5 bound ligands:
Ligand FE2 1 x FE2
Ligand SIN 1 x SIN
Ligand ARG 1 x ARG
Ligand EDO 1 x EDO
Ligand PEG 1 x PEG
1 modified residue:
Ligand MHS 1 x MHS

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I03
Spacegroup: C2
Unit cell:
a: 81.145Å b: 67.107Å c: 62.945Å
α: 90° β: 109.221° γ: 90°
R-values:
R R work R free
0.159 0.158 0.187
Expression system: Escherichia coli

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