4b5i

X-ray diffraction
2.56Å resolution

Product complex of Neisseria AP endonuclease in presence of metal ions

Released:

Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero tetramer (preferred)
Entry contents:
1 distinct polypeptide molecule
3 distinct DNA molecules
Macromolecules (4 distinct):
Endo/exonuclease/phosphatase domain-containing protein Chain: A
Molecule details ›
Chain: A
Length: 259 amino acids
Theoretical weight: 29.7 KDa
Source organism: Neisseria meningitidis
Expression system: Escherichia coli
UniProt:
  • Canonical: Q7DD47 (Residues: 1-259; Coverage: 100%)
Gene names: NMB2082, exoA
Sequence domains: Endonuclease/Exonuclease/phosphatase family
Structure domains: Endonuclease/exonuclease/phosphatase
5'-D(*GP*CP*TP*AP*CP)-3' Chain: U
Molecule details ›
Chain: U
Length: 5 nucleotides
Theoretical weight: 1.48 KDa
Source organism: Neisseria meningitidis
Expression system: Not provided
5'-D(*CP*GP*AP*TP*GP*GP*GP*TP*AP*GP*CP)-3' Chain: V
Molecule details ›
Chain: V
Length: 11 nucleotides
Theoretical weight: 3.41 KDa
Source organism: Neisseria meningitidis
Expression system: Not provided
5'-D(*3DRP*CP*AP*TP*CP*GP)-3' Chain: X
Molecule details ›
Chain: X
Length: 6 nucleotides
Theoretical weight: 1.66 KDa
Source organism: Neisseria meningitidis
Expression system: Not provided

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I03
Spacegroup: P43212
Unit cell:
a: 69.09Å b: 69.09Å c: 119.67Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.207 0.205 0.252
Expression systems:
  • Escherichia coli
  • Not provided