X-ray diffraction
1.65Å resolution

Crystal structure of the catalytic domain of DapE protein from V.cholerea in the Zn bound form


Function and Biology Details

Reaction catalysed:
N-succinyl-LL-2,6-diaminoheptanedioate + H(2)O = succinate + LL-2,6-diaminoheptanedioate
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Succinyl-diaminopimelate desuccinylase Chains: A, B
Molecule details ›
Chains: A, B
Length: 268 amino acids
Theoretical weight: 28.68 KDa
Source organism: Vibrio cholerae O1 biovar El Tor str. N16961
Expression system: Escherichia coli BL21(DE3)
  • Canonical: Q9KQ52 (Residues: 2-181, 295-377; Coverage: 70%)
Gene names: VC_2152, dapE
Sequence domains: Peptidase family M20/M25/M40
Structure domains: Zn peptidases

Ligands and Environments

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-ID
Spacegroup: P32
Unit cell:
a: 49.898Å b: 49.898Å c: 231.762Å
α: 90° β: 90° γ: 120°
R R work R free
0.145 0.141 0.166
Expression system: Escherichia coli BL21(DE3)