› 4mdf

X-ray diffraction
1.73Å resolution

Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
hetero tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-107084 (preferred)
Entry contents:
1 distinct polypeptide molecule
1 distinct DNA molecule
Macromolecules (2 distinct):
Metallophosphoesterase Chains: A, B
Molecule details ›
Chains: A, B
Length: 171 amino acids
Theoretical weight: 19.49 KDa
Source organism: Acetivibrio thermocellus ATCC 27405
Expression system: Escherichia coli
UniProt:
  • Canonical: A3DJ38 (Residues: 1-170; Coverage: 20%)
Gene name: Cthe_2768
Sequence domains: AAA domain
Structure domains: P-loop containing nucleotide triphosphate hydrolases
DNA (5'-D(*CP*CP*TP*GP*T)-3') Chains: C, D
Molecule details ›
Chains: C, D
Length: 5 nucleotides
Theoretical weight: 1.47 KDa
Source organism: Acetivibrio thermocellus ATCC 27405
Expression system: Not provided

Ligands and Environments

3 bound ligands:
Ligand GTP 2 x GTP
Ligand MG 2 x MG
Ligand CIT 1 x CIT
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X25
Spacegroup: P212121
Unit cell:
a: 53.025Å b: 72.755Å c: 119.46Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.166 0.163 0.196
Expression systems:
  • Escherichia coli
  • Not provided

Quick links

Citations

1 review citation

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

3 mentions without citation

Structures of bacterial polynucleotide kinase in a Michaelis complex with GTP•Mg2+ and 5'-OH oligonucleotide and a product complex with GDP•Mg2+ and 5'-PO4 oligonucleotide reveal a mechanism of general acid-base catalysis and the determinants of phosphoacceptor recognition.
Das et al. (2014)
2 more