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› 6ma1

X-ray diffraction
2.75Å resolution

Crystal structure of human O-GlcNAc transferase bound to a peptide from HCF-1 pro-repeat 2 (11-26) and inhibitor 4a

Released:
DOI: 10.2210/pdb6ma1/pdb
Model geometry
Fit model/data
PDB entry 6ma1 coloured by chain, front view.
PDB entry 6ma1 coloured by chain, side view.
PDB entry 6ma1 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structure-Based Evolution of Low Nanomolar O-GlcNAc Transferase Inhibitors.
Martin SES, Tan ZW, Itkonen HM, Duveau DY, Paulo JA, Janetzko J, Boutz PL, Törk L, Moss FA, Thomas CJ, Gygi SP, Lazarus MB, Walker S
J Am Chem Soc 140 13542-13545 (2018)
PMID: 30285435

Function and Biology Details

Reaction catalysed: 
(1) L-seryl-[protein] + UDP-N-acetyl-alpha-D-glucosamine = 3-O-(N-acetyl-beta-D-glucosaminyl)-L-seryl-[protein] + UDP + H(+).
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-127411 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit Chain: A
Molecule details ›
Chain: A
Length: 723 amino acids
Theoretical weight: 80.97 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: O15294 (Residues: 323-1041; Coverage: 69%)
Gene name: OGT
Sequence domains:
HCF C-terminal chain 2 Chain: B
Molecule details ›
Chain: B
Length: 16 amino acids
Theoretical weight: 1.61 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: P51610 (Residues: 1082-1097; Coverage: 1%)
Gene names: HCF1, HCFC1, HFC1

Ligands and Environments

1 bound ligand:
Ligand JA4 1 x JA4
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: APS BEAMLINE 24-ID-E
Spacegroup: P3221
Unit cell:
a: 100.303Å b: 100.303Å c: 130.301Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.201 0.199 0.24
Expression systems:
  • Escherichia coli BL21(DE3)
  • Not provided

Quick links

Citations

14 review citations

Role of O-Linked N-Acetylglucosamine Protein Modification in Cellular (Patho)Physiology.
Chatham et al. (2021)
13 more

3 mentions without citation

Molecular Interrogation to Crack the Case of O-GlcNAc.
Estevez et al. (2020)
2 more