7kxh

X-ray diffraction
1.94Å resolution

Dihydrodipicolinate synthase (DHDPS) from C.jejuni with pyruvate bound in the active site and R,R-bislysine bound at the allosteric site in C2221 space group

Released:
Entry authors: Saran S, Sanders DAR

Function and Biology Details

Reaction catalysed:
Pyruvate + L-aspartate-4-semialdehyde = (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinate + H(2)O
Biochemical function:
Cellular component:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
PDBe Complex ID:
PDB-CPX-192936 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
4-hydroxy-tetrahydrodipicolinate synthase Chains: A, B, C, D, E, F
Molecule details ›
Chains: A, B, C, D, E, F
Length: 310 amino acids
Theoretical weight: 34.19 KDa
Source organism: Campylobacter jejuni subsp. jejuni NCTC 11168 = ATCC 700819
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9PPB4 (Residues: 1-298; Coverage: 100%)
Gene names: Cj0806, dapA
Sequence domains: Dihydrodipicolinate synthetase family

Ligands and Environments

1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: CLSI BEAMLINE 08ID-1
Spacegroup: C2221
Unit cell:
a: 85.09Å b: 231.56Å c: 198.62Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.166 0.164 0.192
Expression system: Escherichia coli