› 6vl7

X-ray diffraction
2.14Å resolution

Crystal structure of the H583C mutant of GoxA soaked with glycine

Released:
DOI: 10.2210/pdb6vl7/pdb
PDB entry 6vl7 coloured by chain, front view.
PDB entry 6vl7 coloured by chain, side view.
PDB entry 6vl7 coloured by chain, top view.
Source organism: Pseudoalteromonas luteoviolacea DSM 6061
Primary publication:
Roles of active-site residues in catalysis, substrate binding, cooperativity, and the reaction mechanism of the quinoprotein glycine oxidase.
Mamounis KJ, Yukl ET, Davidson VL
J Biol Chem 295 6472-6481 (2020)
PMID: 32234764

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:
Glycine oxidase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 816 amino acids
Theoretical weight: 91.49 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 10 x SO4
Ligand PEG 1 x PEG
Ligand PGE 3 x PGE
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: 109.811Å b: 93.285Å c: 188.572Å
α: 90° β: 95.08° γ: 90°
R-values:
R R work R free
0.157 0.156 0.211
Expression system: Escherichia coli

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Citations

1 review citation

Lipid-dependent sequential allosteric activation of heat-sensing TRPV1 channels by anchor-stereoselective "hot" vanilloid compounds and analogs.
Wang G. (2021)

1 mention without citation

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