5vvt

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)
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
ETS domain-containing protein Elk-1 Chains: B, D
Molecule details ›
Chains: B, D
Length: 8 amino acids
Theoretical weight: 950 Da
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: P19419 (Residues: 378-385; Coverage: 2%)
Gene name: ELK1

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 21-ID-F
Spacegroup: P21
Unit cell:
a: 82.363Å b: 95.793Å c: 89.323Å
α: 90° β: 114.51° γ: 90°
R-values:
R R work R free
0.215 0.211 0.291
Expression systems:
  • Escherichia coli
  • Not provided