› 6oha

X-ray diffraction
2.21Å resolution

Yeast Guanine Deaminase

Released:
DOI: 10.2210/pdb6oha/pdb
PDB entry 6oha coloured by chain, front view.
PDB entry 6oha coloured by chain, side view.
PDB entry 6oha coloured by chain, top view.
Source organism: Saccharomyces cerevisiae S288C
Primary publication:
Structural Determinants for Substrate Selectivity in Guanine Deaminase Enzymes of the Amidohydrolase Superfamily.
Shek R, Hilaire T, Sim J, French JB
Biochemistry 58 3280-3292 (2019)
PMID: 31283204

Function and Biology Details

Reaction catalysed: 
Guanine + H(2)O = xanthine + NH(3)
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-170495 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Probable guanine deaminase Chain: A
Molecule details ›
Chain: A
Length: 489 amino acids
Theoretical weight: 55.27 KDa
Source organism: Saccharomyces cerevisiae S288C
Expression system: Escherichia coli
UniProt:
  • Canonical: Q07729 (Residues: 1-489; Coverage: 100%)
Gene names: GUD1, YDL238C
Sequence domains: Amidohydrolase family

Ligands and Environments

4 bound ligands:
Ligand XAN 1 x XAN
Ligand ZN 1 x ZN
Ligand 1PE 3 x 1PE
Ligand SO4 3 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS-II BEAMLINE 17-ID-1
Spacegroup: P4322
Unit cell:
a: 106.812Å b: 106.812Å c: 114.178Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.158 0.156 0.203
Expression system: Escherichia coli

Quick links

Citations

7 citation in other articles

Unfolding New Roles for Guanine-Based Purines and Their Metabolizing Enzymes in Cancer and Aging Disorders.
Di Iorio et al. (2021)
6 more

1 mention without citation

Structural Determinants for Substrate Selectivity in Guanine Deaminase Enzymes of the Amidohydrolase Superfamily.
Shek et al. (2019)