› 1arz

X-ray diffraction
2.6Å resolution

ESCHERICHIA COLI DIHYDRODIPICOLINATE REDUCTASE IN COMPLEX WITH NADH AND 2,6 PYRIDINE DICARBOXYLATE

Released:
DOI: 10.2210/pdb1arz/pdb
PDB entry 1arz coloured by chain, front view.
PDB entry 1arz coloured by chain, side view.
PDB entry 1arz coloured by chain, top view.
Source organism: Escherichia coli K-12
Primary publication:
Three-dimensional structure of Escherichia coli dihydrodipicolinate reductase in complex with NADH and the inhibitor 2,6-pyridinedicarboxylate.
Scapin G, Reddy SG, Zheng R, Blanchard JS
Biochemistry 36 15081-8 (1997)
PMID: 9398235

Function and Biology Details

Reaction catalysed: 
(S)-2,3,4,5-tetrahydropyridine-2,6-dicarboxylate + NAD(P)(+) + H(2)O = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + NAD(P)H
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-137326 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
4-hydroxy-tetrahydrodipicolinate reductase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 273 amino acids
Theoretical weight: 28.79 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P04036 (Residues: 1-273; Coverage: 100%)
Gene names: JW0029, b0031, dapB
Sequence domains:
Structure domains:

Ligands and Environments


Cofactor: Ligand NAI 3 x NAI
3 bound ligands:
Ligand PO4 1 x PO4
Ligand K 2 x K
Ligand PDC 3 x PDC
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RUH2R
Spacegroup: P212121
Unit cell:
a: 137.6Å b: 123.8Å c: 66.6Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.214 0.214 0.297
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

1 review citation

Bacterial diaminopimelate metabolism as a target for antibiotic design.
Cox et al. (2000)
18 other articles

10 mentions without citation

Coupling between catalytic site and collective dynamics: a requirement for mechanochemical activity of enzymes.
Yang et al. (2005)
9 more