› 4zxl

X-ray diffraction
2.6Å resolution

CpOGA D298N in complex with Drosophila HCF -derived Thr-O-GlcNAc peptide

Released:
DOI: 10.2210/pdb4zxl/pdb
PDB entry 4zxl coloured by chain, front view.
PDB entry 4zxl coloured by chain, side view.
PDB entry 4zxl coloured by chain, top view.
Source organisms:
Primary publication:
A mutant O-GlcNAcase as a probe to reveal global dynamics of protein O-GlcNAcylation during Drosophila embryonic development.
Mariappa D, Selvan N, Borodkin V, Alonso J, Ferenbach AT, Shepherd C, Navratilova IH, vanAalten DMF
Biochem J 470 255-262 (2015)
PMID: 26348912

Function and Biology Details

Reaction catalysed: 
[Protein]-3-O-(N-acetyl-beta-D-glucosaminyl)-L-serine + H(2)O = [protein]-L-serine + N-acetyl-D-glucosamine
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-165416 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
NAG-PRO-SER-THR-ALA-Thr-O-GlcNAc containing peptide from drosophila HCF Chain: H
Molecule details ›
Chain: H
Length: 4 amino acids
Theoretical weight: 374 Da
Source organism: Drosophila melanogaster
Expression system: Not provided
O-GlcNAcase NagJ Chain: A
Molecule details ›
Chain: A
Length: 579 amino acids
Theoretical weight: 65.1 KDa
Source organism: Clostridium perfringens ATCC 13124
Expression system: Escherichia coli
UniProt:
  • Canonical: Q0TR53 (Residues: 39-617; Coverage: 60%)
Gene names: CPF_1442, nagJ
Sequence domains:
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand NAG 1 x NAG
Ligand CD 15 x CD
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID23-1
Spacegroup: P61
Unit cell:
a: 118.56Å b: 118.56Å c: 148.441Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.172 0.171 0.22
Expression systems:
  • Not provided
  • Escherichia coli

Quick links

Citations

13 review citations

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

1 mention without citation

A mutant O-GlcNAcase as a probe to reveal global dynamics of protein O-GlcNAcylation during Drosophila embryonic development.
Mariappa et al. (2015)