PDBe 5un8

X-ray diffraction
2.13Å resolution

Crystal Structure of human O-GlcNAcase in complex with glycopeptide p53

Released:
Source organism: Homo sapiens
Primary publication:
Structures of human O-GlcNAcase and its complexes reveal a new substrate recognition mode.
Nat. Struct. Mol. Biol. (2017)
PMID: 28319083

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, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 504 amino acids
Theoretical weight: 57.82 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli-Pichia pastoris shuttle vector pPpARG4
UniProt:
  • 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
Cellular tumor antigen p53 Chains: E, F, G, H
Molecule details ›
Chains: E, F, G, H
Length: 11 amino acids
Theoretical weight: 1.2 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: P04637 (Residues: 144-154; Coverage: 3%)
Gene names: P53, TP53

Ligands and Environments

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 21-ID-D
Spacegroup: P21
Unit cell:
a: 89.909Å b: 95.393Å c: 149.32Å
α: 90° β: 96.91° γ: 90°
R-values:
R R work R free
0.187 0.184 0.229
Expression systems:
  • Escherichia coli-Pichia pastoris shuttle vector pPpARG4
  • Not provided