PDBe 5vvx

X-ray diffraction
2.9Å resolution

Structural Investigations of the Substrate Specificity of Human O-GlcNAcase


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
  • Canonical: O60502 (Residues: 60-400, 553-704; Coverage: 54%)
  • Best match: O60502-4 (Residues: 60-483, 500-651)
Gene names: HEXC, KIAA0679, MEA5, MGEA5, OGA
Sequence domains: beta-N-acetylglucosaminidase
Lamin-B1 Chains: B, D
Molecule details ›
Chains: B, D
Length: 13 amino acids
Theoretical weight: 1.35 KDa
Source organism: Homo sapiens
Expression system: Not provided
  • Canonical: P20700 (Residues: 389-401; Coverage: 2%)
Gene names: LMN2, LMNB, LMNB1

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: 82.922Å b: 96.222Å c: 89.653Å
α: 90° β: 114.56° γ: 90°
R R work R free
0.204 0.2 0.282
Expression systems:
  • Escherichia coli
  • Not provided