5bnw

X-ray diffraction
2.4Å resolution

The active site of O-GlcNAc transferase imposes constraints on substrate sequence

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
UniProt:
  • Canonical: O15294 (Residues: 323-1041; Coverage: 69%)
  • Best match: O15294-4 (Residues: 1-660)
Gene name: OGT
Sequence domains:
Structure domains:
Lamin-B2 Chain: D
Molecule details ›
Chain: D
Length: 13 amino acids
Theoretical weight: 1.35 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: Q03252 (Residues: 403-415; Coverage: 2%)
Gene names: LMN2, LMNB2

Ligands and Environments

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I04-1
Spacegroup: F222
Unit cell:
a: 138.183Å b: 150.176Å c: 199.241Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.19 0.187 0.235
Expression systems:
  • Escherichia coli BL21
  • Not provided