› 6ubr

X-ray diffraction
1.96Å resolution

Crystal structure of D678A GoxA bound to glycine at pH 7.5

Released:
DOI: 10.2210/pdb6ubr/pdb
PDB entry 6ubr coloured by chain, front view.
PDB entry 6ubr coloured by chain, side view.
PDB entry 6ubr coloured by chain, top view.
Source organism: Pseudoalteromonas luteoviolacea DSM 6061
Primary publication:
Kinetic and structural evidence that Asp-678 plays multiple roles in catalysis by the quinoprotein glycine oxidase.
Mamounis KJ, Avalos D, Yukl ET, Davidson VL
J Biol Chem 294 17463-17470 (2019)
PMID: 31615898

Function and Biology Details

Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-103073 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Uncharacterized protein Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 816 amino acids
Theoretical weight: 91.48 KDa
Source organism: Pseudoalteromonas luteoviolacea DSM 6061
Expression system: Escherichia coli
UniProt:
  • Canonical: A0A161XU12 (Residues: 1-816; Coverage: 100%)
Gene name: N475_19905
Sequence domains:

Ligands and Environments

4 bound ligands:
Ligand MG 4 x MG
Ligand SO4 2 x SO4
Ligand PEG 1 x PEG
Ligand GLY 4 x GLY
1 modified residue:
Ligand TRQ 4 x TRQ

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 5.0.2
Spacegroup: P21
Unit cell:
a: 110.679Å b: 93.348Å c: 187.853Å
α: 90° β: 94.95° γ: 90°
R-values:
R R work R free
0.176 0.175 0.209
Expression system: Escherichia coli

Quick links

Citations

2 citation in other articles

Roles of active-site residues in catalysis, substrate binding, cooperativity, and the reaction mechanism of the quinoprotein glycine oxidase.
Mamounis et al. (2020)
1 more

1 mention without citation

Kinetic and structural evidence that Asp-678 plays multiple roles in catalysis by the quinoprotein glycine oxidase.
Mamounis et al. (2019)