› 5m7u

X-ray diffraction
2.3Å resolution

Structure of human O-GlcNAc hydrolase with new iminocyclitol type inhibitor

Released:
DOI: 10.2210/pdb5m7u/pdb
PDB entry 5m7u coloured by chain, front view.
PDB entry 5m7u coloured by chain, side view.
PDB entry 5m7u coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structural and functional insight into human O-GlcNAcase.
Roth C, Chan S, Offen WA, Hemsworth GR, Willems LI, King DT, Varghese V, Britton R, Vocadlo DJ, Davies GJ
Nat Chem Biol 13 610-612 (2017)
PMID: 28346405

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:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-130001 (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

1 bound ligand:
Ligand XHA 2 x XHA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I04
Spacegroup: P43212
Unit cell:
a: 101.23Å b: 101.23Å c: 284.673Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.201 0.2 0.227
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

25 review citations

Protein O-GlcNAcylation: emerging mechanisms and functions.
Yang et al. (2017)
24 more

3 mentions without citation

Molecular Interrogation to Crack the Case of O-GlcNAc.
Estevez et al. (2020)
2 more