5vvu

X-ray diffraction
2.7Å 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-130007 (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
TGF-beta-activated kinase 1 and MAP3K7-binding protein 1 Chains: B, D
Molecule details ›
Chains: B, D
Length: 7 amino acids
Theoretical weight: 751 Da
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: Q15750 (Residues: 392-398; Coverage: 1%)
Gene names: MAP3K7IP1, TAB1

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: 82.507Å b: 96.06Å c: 88.968Å
α: 90° β: 114.51° γ: 90°
R-values:
R R work R free
0.211 0.208 0.275
Expression systems:
  • Escherichia coli
  • Not provided