› 6tka

X-ray diffraction
1.91Å resolution

Crystal structure of human O-GlcNAc transferase bound to substrate 7 and a peptide from HCF-1 pro-repeat 2 (11-26)

Released:
DOI: 10.2210/pdb6tka/pdb
PDB entry 6tka coloured by chain, front view.
PDB entry 6tka coloured by chain, side view.
PDB entry 6tka coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
A Direct Fluorescent Activity Assay for Glycosyltransferases Enables Convenient High-Throughput Screening: Application to O-GlcNAc Transferase.
Alteen MG, Gros C, Meek RW, Cardoso DA, Busmann JA, Sangouard G, Deen MC, Tan HY, Shen DL, Russell CC, Davies GJ, Robinson PJ, McCluskey A, Vocadlo DJ
Angew Chem Int Ed Engl 59 9601-9609 (2020)
PMID: 32092778

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:
hetero dimer (preferred)
hetero tetramer
Assembly name:
PDBe Complex ID:
PDB-CPX-127417 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit Chain: AAA
Molecule details ›
Chain: AAA
Length: 727 amino acids
Theoretical weight: 81.39 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: O15294 (Residues: 323-1046; Coverage: 69%)
Gene name: OGT
Sequence domains:
HCF-1 pro-repeat 2 (11-26) Chain: BBB
Molecule details ›
Chain: BBB
Length: 16 amino acids
Theoretical weight: 1.61 KDa
Source organism: Homo sapiens
Expression system: Not provided

Ligands and Environments

2 bound ligands:
Ligand NJ5 1 x NJ5
Ligand NG8 1 x NG8
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I04-1
Spacegroup: P3221
Unit cell:
a: 100.859Å b: 100.859Å c: 132.629Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.187 0.184 0.233
Expression systems:
  • Escherichia coli BL21(DE3)
  • Not provided

Quick links

Citations

2 review citations

Role of glycosylation in TGF-β signaling and epithelial-to-mesenchymal transition in cancer.
Zhang et al. (2021)
1 more