1w3b

X-ray diffraction
2.85Å resolution

The superhelical TPR domain of O-linked GlcNAc transferase reveals structural similarities to importin alpha.

Released:

Function and Biology Details

Reaction catalysed:
UDP-N-acetyl-alpha-D-glucosamine + [protein]-L-serine = UDP + [protein]-3-O-(N-acetyl-beta-D-glucosaminyl)-L-serine
Biochemical function:
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit Chains: A, B
Molecule details ›
Chains: A, B
Length: 388 amino acids
Theoretical weight: 43.51 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: O15294 (Residues: 23-410; Coverage: 37%)
Gene name: OGT
Sequence domains:
Structure domains: Tetratricopeptide repeat domain

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-2
Spacegroup: P1
Unit cell:
a: 64.32Å b: 75.51Å c: 77.67Å
α: 105.08° β: 105.14° γ: 110.28°
R-values:
R R work R free
0.259 0.259 0.297
Expression system: Escherichia coli BL21(DE3)