2wzi

X-ray diffraction
1.9Å resolution

BtGH84 D243N in complex with 5F-oxazoline

Released:
Primary publication:
Visualizing the reaction coordinate of an O-GlcNAc hydrolase.
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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
O-GlcNAcase BT_4395 Chains: A, B
Molecule details ›
Chains: A, B
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


No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-4
Spacegroup: P1
Unit cell:
a: 51.38Å b: 93.82Å c: 98.88Å
α: 104.14° β: 94.06° γ: 103.08°
R-values:
R R work R free
0.186 0.184 0.223
Expression system: Escherichia coli BL21