7kuz

X-ray diffraction
2.25Å resolution

Dihydrodipicolinate synthase (DHDPS) from C.jejuni, H56N mutant with pyruvate bound in the active site and L-lysine bound at the allosteric site

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

Assemblies composition:
hetero tetramer (preferred)
homo tetramer
PDBe Complex ID:
PDB-CPX-192933 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
4-hydroxy-tetrahydrodipicolinate synthase Chains: A, B, C, D, F
Molecule details ›
Chains: A, B, C, D, F
Length: 310 amino acids
Theoretical weight: 34.16 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
4-hydroxy-tetrahydrodipicolinate synthase Chain: E
Molecule details ›
Chain: E
Length: 310 amino acids
Theoretical weight: 34.09 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

Experiments and Validation Details

Entry percentile scores
X-ray source: CLSI BEAMLINE 08ID-1
Spacegroup: C2221
Unit cell:
a: 86.047Å b: 227.328Å c: 202.278Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.18 0.178 0.218
Expression system: Escherichia coli