› 5bnw

X-ray diffraction
2.4Å resolution

The active site of O-GlcNAc transferase imposes constraints on substrate sequence

Released:
DOI: 10.2210/pdb5bnw/pdb
PDB entry 5bnw coloured by chain, front view.
PDB entry 5bnw coloured by chain, side view.
PDB entry 5bnw coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
The active site of O-GlcNAc transferase imposes constraints on substrate sequence.
Pathak S, Alonso J, Schimpl M, Rafie K, Blair DE, Borodkin VS, Albarbarawi O, van Aalten DMF, van Aalten DM
Nat Struct Mol Biol 22 744-750 (2015)
PMID: 26237509

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-127418 (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
UniProt:
  • Canonical: O15294 (Residues: 323-1041; Coverage: 69%)
Gene name: OGT
Sequence domains:
Structure domains:
Lamin-B2 Chain: D
Molecule details ›
Chain: D
Length: 13 amino acids
Theoretical weight: 1.35 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: Q03252 (Residues: 403-415; Coverage: 2%)
Gene names: LMN2, LMNB2

Ligands and Environments

1 bound ligand:
Ligand 12V 1 x 12V
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I04-1
Spacegroup: F222
Unit cell:
a: 138.183Å b: 150.176Å c: 199.241Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.19 0.187 0.235
Expression systems:
  • Escherichia coli BL21
  • Not provided

Quick links

Citations

26 review citations

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

3 mentions without citation

The active site of O-GlcNAc transferase imposes constraints on substrate sequence.
Pathak et al. (2015)
2 more