› 1s5v

X-ray diffraction
2.35Å resolution

Crystal Structure Analysis of a mutant of DIHYDRODIPICOLINATE SYNTHASE--residue Tyr107 to Phe107

Released:
DOI: 10.2210/pdb1s5v/pdb
PDB entry 1s5v coloured by chain, front view.
PDB entry 1s5v coloured by chain, side view.
PDB entry 1s5v coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
The crystal structure of three site-directed mutants of Escherichia coli dihydrodipicolinate synthase: further evidence for a catalytic triad.
Dobson RC, Valegård K, Gerrard JA
J Mol Biol 338 329-39 (2004)
PMID: 15066435

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:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assemblies composition:
homo tetramer
homo dimer
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-141375 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
4-hydroxy-tetrahydrodipicolinate synthase Chains: A, B
Molecule details ›
Chains: A, B
Length: 292 amino acids
Theoretical weight: 31.29 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P0A6L2 (Residues: 1-292; Coverage: 100%)
Gene names: JW2463, b2478, dapA
Sequence domains: Dihydrodipicolinate synthetase family
Structure domains: Aldolase class I

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU
Spacegroup: P3121
Unit cell:
a: 120.888Å b: 120.888Å c: 110.202Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.197 0.195 0.232
Expression system: Escherichia coli

Quick links

Citations

5 review citations

Structure, dynamics, assembly, and evolution of protein complexes.
Marsh et al. (2015)
4 more

1 mention without citation

Insight into de-regulation of amino acid feedback inhibition: a focus on structure analysis method.
Naz et al. (2023)