5vvv

X-ray diffraction
2.8Å resolution

Structural Investigations of the Substrate Specificity of Human O-GlcNAcase

Released:

Function and Biology Details

Reaction catalysed:
[Protein]-3-O-(N-acetyl-beta-D-glucosaminyl)-L-serine + H(2)O = [protein]-L-serine + N-acetyl-D-glucosamine
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
hetero tetramer (preferred)
PDBe Complex ID:
PDB-CPX-130003 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Protein O-GlcNAcase Chains: A, C
Molecule details ›
Chains: A, C
Length: 504 amino acids
Theoretical weight: 57.82 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: O60502 (Residues: 60-400, 553-704; Coverage: 54%)
Gene names: HEXC, KIAA0679, MEA5, MGEA5, OGA
Sequence domains: beta-N-acetylglucosaminidase
Structure domains: Glycosidases
Alpha-crystallin B chain Chains: B, D
Molecule details ›
Chains: B, D
Length: 13 amino acids
Theoretical weight: 1.52 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: P02511 (Residues: 38-50; Coverage: 7%)
Gene names: CRYA2, CRYAB, HSPB5

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 21-ID-G
Spacegroup: P21
Unit cell:
a: 83.084Å b: 96.258Å c: 89.809Å
α: 90° β: 114.29° γ: 90°
R-values:
R R work R free
0.199 0.196 0.257
Expression systems:
  • Escherichia coli
  • Not provided