› 5abg

X-ray diffraction
2Å resolution

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:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-183580 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
O-GlcNAcase BT_4395 Chains: A, B
Molecule details ›
Chains: A, B
Length: 726 amino acids
Theoretical weight: 83.51 KDa
Source organism: Bacteroides thetaiotaomicron
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q89ZI2 (Residues: 22-737; Coverage: 100%)
Gene name: BT_4395
Sequence domains:
Structure domains:

Ligands and Environments

3 bound ligands:
Ligand EDO 2 x EDO
Ligand V0N 2 x V0N
Ligand CA 1 x CA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I04
Unit cell:
a: 51.531Å b: 161.184Å c: 223.98Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.206 0.204 0.235
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

6 review citations

Deciphering the Functions of Protein O-GlcNAcylation with Chemistry.
Worth et al. (2017)
5 more