› 4gz6

X-ray diffraction
2.98Å resolution

Crystal structure of human O-GlcNAc Transferase with UDP-5SGlcNAc

Released:
DOI: 10.2210/pdb4gz6/pdb
PDB entry 4gz6 coloured by chain, front view.
PDB entry 4gz6 coloured by chain, side view.
PDB entry 4gz6 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structural snapshots of the reaction coordinate for O-GlcNAc transferase.
Lazarus MB, Jiang J, Gloster TM, Zandberg WF, Whitworth GE, Vocadlo DJ, Walker S
Nat Chem Biol 8 966-8 (2012)
PMID: 23103939

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:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assemblies composition:
monomeric (preferred)
homo dodecamer
Assembly name:
PDBe Complex ID:
PDB-CPX-127409 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 723 amino acids
Theoretical weight: 80.97 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: O15294 (Residues: 323-1041; Coverage: 69%)
Gene name: OGT
Sequence domains:
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand 12V 4 x 12V
Ligand SO4 17 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X25
Spacegroup: P321
Unit cell:
a: 272.338Å b: 272.338Å c: 143.46Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.198 0.197 0.223
Expression system: Escherichia coli

Quick links

Citations

20 review citations

Protein O-GlcNAcylation in diabetes and diabetic complications.
Ma et al. (2013)
19 more

2 mentions without citation

Structural snapshots of the reaction coordinate for O-GlcNAc transferase.
Lazarus et al. (2012)
1 more