4e6n

X-ray diffraction
2.39Å resolution

Crystal structure of bacterial Pnkp-C/Hen1-N heterodimer

Released:

Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
PDBe Complex ID:
PDB-CPX-107079 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Metallophosphoesterase Chains: A, C
Molecule details ›
Chains: A, C
Length: 427 amino acids
Theoretical weight: 48.88 KDa
Source organism: Acetivibrio thermocellus ATCC 27405
Expression system: Escherichia coli
UniProt:
  • Canonical: A3DJ38 (Residues: 445-870; Coverage: 49%)
Gene name: Cthe_2768
Sequence domains: PNKP adenylyltransferase domain, ligase domain
Structure domains:
Small RNA 2'-O-methyltransferase Chains: B, D
Molecule details ›
Chains: B, D
Length: 230 amino acids
Theoretical weight: 26.24 KDa
Source organism: Acetivibrio thermocellus ATCC 27405
Expression system: Escherichia coli
UniProt:
  • Canonical: A3DJ37 (Residues: 1-230; Coverage: 50%)
Gene name: Cthe_2767
Sequence domains: RNA repair, ligase-Pnkp-associating, region of Hen1
Structure domains: Hen1, N-terminal domain

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 21-ID-G
Spacegroup: P1
Unit cell:
a: 59.63Å b: 59.695Å c: 101.54Å
α: 81.38° β: 87.82° γ: 88.82°
R-values:
R R work R free
0.17 0.168 0.222
Expression system: Escherichia coli