› 4n3a

X-ray diffraction
1.88Å resolution

Crystal Structure of human O-GlcNAc transferase bound to a peptide from HCF-1 pro-repeat 2 (1-26)E10A

Released:
DOI: 10.2210/pdb4n3a/pdb
PDB entry 4n3a coloured by chain, front view.
PDB entry 4n3a coloured by chain, side view.
PDB entry 4n3a coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
HCF-1 is cleaved in the active site of O-GlcNAc transferase.
Lazarus MB, Jiang J, Kapuria V, Bhuiyan T, Janetzko J, Zandberg WF, Vocadlo DJ, Herr W, Walker S
Science 342 1235-9 (2013)
PMID: 24311690

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:
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:
Structure domains:
HCF C-terminal chain 2 Chain: B
Molecule details ›
Chain: B
Length: 26 amino acids
Theoretical weight: 2.64 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: P51610 (Residues: 1072-1097; Coverage: 1%)
Gene names: HCF1, HCFC1, HFC1

Ligands and Environments

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

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X29A
Spacegroup: P6122
Unit cell:
a: 98.929Å b: 98.929Å c: 367.015Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.202 0.2 0.222
Expression systems:
  • Escherichia coli BL21(DE3)
  • Not provided

Quick links

Citations

35 review citations

Protein O-GlcNAcylation: emerging mechanisms and functions.
Yang et al. (2017)
34 more

5 mentions without citation

Structural characterization of the O-GlcNAc cycling enzymes: insights into substrate recognition and catalytic mechanisms.
Joiner et al. (2019)
4 more