X-ray diffraction
1.8Å resolution

Structure of a hydrolase bound with an inhibitor


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:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
O-GlcNAcase BT_4395 Chains: A, B
Molecule details ›
Chains: A, B
Length: 716 amino acids
Theoretical weight: 82.32 KDa
Source organism: Bacteroides thetaiotaomicron
Expression system: Escherichia coli BL21
  • Canonical: Q89ZI2 (Residues: 22-737; Coverage: 100%)
Gene name: BT_4395
Sequence domains:
Structure domains:

Ligands and Environments

2 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-1
Spacegroup: P1
Unit cell:
a: 51.44Å b: 93.69Å c: 99.02Å
α: 104.07° β: 94.18° γ: 102.97°
R R work R free
0.213 0.211 0.249
Expression system: Escherichia coli BL21