4n39

X-ray diffraction
1.76Å resolution

Crystal structure of human O-GlcNAc transferase bound to a peptide from HCF-1 pro-repeat 2 (11-26)

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
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit Chain: A
Molecule details ›
Chain: A
Length: 723 amino acids
Theoretical weight: 80.97 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: O15294 (Residues: 323-1041; Coverage: 69%)
  • Best match: O15294-4 (Residues: 1-660)
Gene name: OGT
Sequence domains:
Structure domains:
HCF C-terminal chain 2 Chain: B
Molecule details ›
Chain: B
Length: 16 amino acids
Theoretical weight: 1.61 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: P51610 (Residues: 1082-1097; Coverage: 1%)
Gene names: HCF1, HCFC1, HFC1

Ligands and Environments

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X29A
Spacegroup: P3221
Unit cell:
a: 101.17Å b: 101.17Å c: 131.73Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.189 0.187 0.216
Expression systems:
  • Escherichia coli BL21(DE3)
  • Not provided