5uej

X-ray diffraction
1.3Å resolution

1.30 A crystal structure of DapE enzyme from Neisseria meningitidis MC58

Released:
Source organism: Neisseria meningitidis
Entry authors: Nocek B, Joachimiak A, Anderson WF, Center for Structural Genomics of Infectious Diseases (CSGID)

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
PDBe Complex ID:
PDB-CPX-191694 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Succinyl-diaminopimelate desuccinylase Chains: A, B
Molecule details ›
Chains: A, B
Length: 384 amino acids
Theoretical weight: 41.65 KDa
Source organism: Neisseria meningitidis
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9JYL2 (Residues: 1-381; Coverage: 100%)
Gene names: NMB1530, dapE
Sequence domains:
Structure domains:

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-ID
Spacegroup: P212121
Unit cell:
a: 74.767Å b: 88.644Å c: 133.402Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.115 0.113 0.153
Expression system: Escherichia coli