› 4cdr

X-ray diffraction
3.15Å resolution

Human O-GlcNAc transferase in complex with a bisubstrate inhibitor, Goblin1

Released:
DOI: 10.2210/pdb4cdr/pdb
PDB entry 4cdr coloured by chain, front view.
PDB entry 4cdr coloured by chain, side view.
PDB entry 4cdr coloured by chain, top view.
Source organisms:
Primary publication:
Bisubstrate UDP-peptide conjugates as human O-GlcNAc transferase inhibitors.
Borodkin VS, Schimpl M, Gundogdu M, Rafie K, Dorfmueller HC, Robinson DA, van Aalten DM
OpenAccess logo Biochem J 457 497-502 (2014)
PMID: 24256146

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:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-518482 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
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 BL21
UniProt:
  • Canonical: O15294 (Residues: 323-1041; Coverage: 69%)
Gene name: OGT
Sequence domains:
Structure domains:
GOBLIN1 Chains: E, F, G, H
Molecule details ›
Chains: E, F, G, H
Length: 9 amino acids
Theoretical weight: 756 Da
Source organism: synthetic construct
Expression system: Not provided

Ligands and Environments

2 bound ligands:
Ligand SO4 31 x SO4
Ligand UDP 4 x UDP
1 modified residue:
Ligand SRZ 4 x SRZ

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID23-1
Spacegroup: P321
Unit cell:
a: 273.728Å b: 273.728Å c: 142.581Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.197 0.197 0.213
Expression systems:
  • Escherichia coli BL21
  • Not provided

Quick links

Citations

14 review citations

Biosynthetic Machinery Involved in Aberrant Glycosylation: Promising Targets for Developing of Drugs Against Cancer.
Vasconcelos-Dos-Santos et al. (2015)
13 more

2 mentions without citation

Bisubstrate UDP-peptide conjugates as human O-GlcNAc transferase inhibitors.
Borodkin et al. (2014)
1 more