› 5lvv

X-ray diffraction
2.54Å resolution

Human OGT in complex with UDP and fused substrate peptide (Tab1)

Released:
DOI: 10.2210/pdb5lvv/pdb
PDB entry 5lvv coloured by chain, front view.
PDB entry 5lvv coloured by chain, side view.
PDB entry 5lvv coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Recognition of a glycosylation substrate by the O-GlcNAc transferase TPR repeats.
Rafie K, Raimi O, Ferenbach AT, Borodkin VS, Kapuria V, van Aalten DMF
Open Biol 7 (2017)
PMID: 28659383

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

Assembly composition:
monomeric (preferred)
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 Chain: A
Molecule details ›
Chain: A
Length: 749 amino acids
Theoretical weight: 83.8 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: O15294 (Residues: 325-1046; Coverage: 69%)
Gene name: OGT
Sequence domains:

Ligands and Environments

2 bound ligands:
Ligand UDP 1 x UDP
Ligand NAG 3 x NAG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID29
Spacegroup: P6122
Unit cell:
a: 98.533Å b: 98.533Å c: 367.2Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.196 0.193 0.245
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

11 review citations

Crosstalk between phosphorylation and O-GlcNAcylation: friend or foe.
van der Laarse et al. (2018)
10 more

3 mentions without citation

Recognition of a glycosylation substrate by the O-GlcNAc transferase TPR repeats.
Rafie et al. (2017)
2 more