› 4xba

X-ray diffraction
1.5Å resolution

Function and Biology Details

Reactions catalysed: 
Adenosine-5'-diphospho-5'-(DNA) + H(2)O = AMP + phospho-5'-(DNA)
(DNA)-3'-diphospho-5'-guanosine + H(2)O = (DNA)-3'-phosphate + GMP
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-130799 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Aprataxin-like protein Chains: A, B
Molecule details ›
Chains: A, B
Length: 200 amino acids
Theoretical weight: 23.23 KDa
Source organism: Schizosaccharomyces pombe 972h-
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: O74859 (Residues: 33-232; Coverage: 86%)
Gene names: SPCC18.09c, hnt3
Sequence domains:
Structure domains: HIT-like

Ligands and Environments

4 bound ligands:
Ligand GMP 1 x GMP
Ligand ZN 2 x ZN
Ligand GOL 1 x GOL
Ligand 5GP 1 x 5GP
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 24-ID-C
Spacegroup: P21
Unit cell:
a: 52.761Å b: 72.509Å c: 53.926Å
α: 90° β: 111.25° γ: 90°
R-values:
R R work R free
0.159 0.157 0.191
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

1 review citation

RNA damage in biological conflicts and the diversity of responding RNA repair systems.
Burroughs et al. (2016)
2 other articles

1 mention without citation

DNA3'pp5'G de-capping activity of aprataxin: effect of cap nucleoside analogs and structural basis for guanosine recognition.
Chauleau et al. (2015)