5m7r

X-ray diffraction
2.35Å resolution

Structure of human O-GlcNAc hydrolase

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Protein O-GlcNAcase Chains: A, B
Molecule details ›
Chains: A, B
Length: 916 amino acids
Theoretical weight: 103.02 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: O60502 (Residues: 1-916; Coverage: 100%)
Gene names: HEXC, KIAA0679, MEA5, MGEA5, OGA
Sequence domains: beta-N-acetylglucosaminidase
Structure domains: Glycosidases

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I04
Spacegroup: P43212
Unit cell:
a: 102.23Å b: 102.23Å c: 285.49Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.217 0.216 0.249
Expression system: Escherichia coli BL21(DE3)