› 6y0n

X-ray diffraction
1.86Å resolution

Arginine hydroxylase VioC in complex with Arg, 2OG and Fe under anaerobic environment using FT-SSX methods

Released:
DOI: 10.2210/pdb6y0n/pdb
PDB entry 6y0n coloured by chain, front view.
PDB entry 6y0n coloured by chain, side view.
PDB entry 6y0n coloured by chain, top view.
Source organism: Streptomyces vinaceus
Primary publication:
Anaerobic fixed-target serial crystallography.
Rabe P, Beale JH, Butryn A, Aller P, Dirr A, Lang PA, Axford DN, Carr SB, Leissing TM, McDonough MA, Davy B, Ebrahim A, Orlans J, Storm SLS, Orville AM, Schofield CJ, Owen RL
IUCrJ 7 901-912 (2020)
PMID: 32939282

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:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-180510 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Alpha-ketoglutarate-dependent L-arginine hydroxylase Chain: A
Molecule details ›
Chain: A
Length: 358 amino acids
Theoretical weight: 39.48 KDa
Source organism: Streptomyces vinaceus
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q6WZB0 (Residues: 1-358; Coverage: 100%)
Gene name: vioC
Sequence domains: Taurine catabolism dioxygenase TauD, TfdA family

Ligands and Environments

3 bound ligands:
Ligand ARG 1 x ARG
Ligand AKG 1 x AKG
Ligand FE 1 x FE
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I24
Spacegroup: C2
Unit cell:
a: 81.99Å b: 66.578Å c: 63.584Å
α: 90° β: 110.15° γ: 90°
R-values:
R R work R free
0.192 0.189 0.228
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

2 review citations

Serial synchrotron and XFEL crystallography for studies of metalloprotein catalysis.
Hough et al. (2021)
1 more

1 mention without citation

Anaerobic fixed-target serial crystallography.
Rabe et al. (2020)