4rg8

X-ray diffraction
2.12Å resolution

Structural and biochemical studies of a moderately thermophilic Exonuclease I from Methylocaldum szegediense

Released:

Function and Biology Details

Reaction catalysed:
Exonucleolytic cleavage in the 3'- to 5'-direction to yield nucleoside 5'-phosphates
Biochemical function:
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-100782 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Exodeoxyribonuclease I Chain: A
Molecule details ›
Chain: A
Length: 523 amino acids
Theoretical weight: 59.28 KDa
Source organism: Methylocaldum szegediense
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: A0A0A0R5X6 (Residues: 1-479; Coverage: 100%)
Sequence domains:
Structure domains:

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I02
Spacegroup: P212121
Unit cell:
a: 60.967Å b: 97.02Å c: 111.411Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.223 0.223 0.253
Expression system: Escherichia coli BL21(DE3)