4b5g

X-ray diffraction
2.75Å resolution

Substrate bound Neisseria AP endonuclease in absence of metal ions (crystal form 2)

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:
hetero trimer (preferred)
Entry contents:
1 distinct polypeptide molecule
2 distinct DNA molecules
Macromolecules (3 distinct):
Exodeoxyribonuclease III Chains: A, B, C
Molecule details ›
Chains: A, B, C
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*(3DR)P*CP*AP*TP*CP*GP)-3' Chains: U, W, Y
Molecule details ›
Chains: U, W, Y
Length: 11 nucleotides
Theoretical weight: 3.19 KDa
Source organism: Neisseria meningitidis
Expression system: Not provided
5'-D(*CP*GP*AP*TP*GP*GP*GP*TP*AP*GP*CP)-3' Chains: V, X, Z
Molecule details ›
Chains: V, X, Z
Length: 11 nucleotides
Theoretical weight: 3.41 KDa
Source organism: Neisseria meningitidis
Expression system: Not provided

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SRS
Spacegroup: P41212
Unit cell:
a: 75.241Å b: 75.241Å c: 380.683Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.233 0.232 0.259
Expression systems:
  • Escherichia coli
  • Not provided