› 2wzh

X-ray diffraction
2.2Å resolution

BtGH84 D242N in complex with MeUMB-derived oxazoline

Released:
DOI: 10.2210/pdb2wzh/pdb
PDB entry 2wzh coloured by chain, front view.
PDB entry 2wzh coloured by chain, side view.
PDB entry 2wzh coloured by chain, top view.
Source organism: Bacteroides thetaiotaomicron VPI-5482
Primary publication:
Visualizing the reaction coordinate of an O-GlcNAc hydrolase.
He Y, Macauley MS, Stubbs KA, Vocadlo DJ, Davies GJ
J Am Chem Soc 132 1807-9 (2010)
PMID: 20067256

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
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 Chain: A
Molecule details ›
Chain: A
Length: 737 amino acids
Theoretical weight: 84.59 KDa
Source organism: Bacteroides thetaiotaomicron VPI-5482
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: Q89ZI2 (Residues: 1-737; Coverage: 100%)
Gene name: BT_4395
Sequence domains:
Structure domains:

Ligands and Environments

3 bound ligands:
Ligand NGO 1 x NGO
Ligand GOL 1 x GOL
Ligand CA 1 x CA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I02
Spacegroup: C2
Unit cell:
a: 184.76Å b: 52.29Å c: 86.93Å
α: 90° β: 100.2° γ: 90°
R-values:
R R work R free
0.188 0.186 0.227
Expression system: Escherichia coli BL21

Quick links

Citations

13 review citations

O-GlcNAc signalling: implications for cancer cell biology.
Slawson et al. (2011)
12 more