› 5lwv

X-ray diffraction
1.9Å resolution

Human OGT in complex with UDP and fused substrate peptide (HCF1)

Released:
DOI: 10.2210/pdb5lwv/pdb
PDB entry 5lwv coloured by chain, front view.
PDB entry 5lwv coloured by chain, side view.
PDB entry 5lwv 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
OpenAccess logo 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:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-127408 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
HCF C-terminal chain 2; UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit Chain: A
Molecule details ›
Chain: A
Length: 749 amino acids
Theoretical weight: 83.78 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P51610 (Residues: 1078-1095; Coverage: 1%)
  • Canonical: O15294 (Residues: 325-1046; Coverage: 69%)
Gene names: HCF1, HCFC1, HFC1, OGT
Sequence domains:

Ligands and Environments

3 bound ligands:
Ligand UDP 1 x UDP
Ligand GOL 1 x GOL
Ligand PO4 2 x PO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID29
Spacegroup: P6222
Unit cell:
a: 168.024Å b: 168.024Å c: 162.265Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.171 0.169 0.199
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

1 mention without citation

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