1o5k

X-ray diffraction
1.8Å resolution

Crystal structure of Dihydrodipicolinate synthase (TM1521) from Thermotoga maritima at 1.80 A resolution

Released:
Source organism: Thermotoga maritima MSB8
Entry author: Joint Center for Structural Genomics (JCSG)

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:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
4-hydroxy-tetrahydrodipicolinate synthase Chains: A, B
Molecule details ›
Chains: A, B
Length: 306 amino acids
Theoretical weight: 33.96 KDa
Source organism: Thermotoga maritima MSB8
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9X1K9 (Residues: 1-294; Coverage: 100%)
Gene names: TM_1521, dapA
Structure domains: Aldolase class I

Ligands and Environments

1 bound ligand:
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 14-BM-C
Spacegroup: C2221
Unit cell:
a: 54.672Å b: 140.768Å c: 155.943Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.142 0.139 0.186
Expression system: Escherichia coli