› 2ehq

X-ray diffraction
1.55Å resolution

Crystal analysis of 1-pyrroline-5-carboxylate dehydrogenase from thermus with bound NADP

Released:
DOI: 10.2210/pdb2ehq/pdb
PDB entry 2ehq coloured by chain, front view.
PDB entry 2ehq coloured by chain, side view.
PDB entry 2ehq coloured by chain, top view.
Source organism: Thermus thermophilus HB8
Primary publication:
New insights into the binding mode of coenzymes: structure of Thermus thermophilus Delta1-pyrroline-5-carboxylate dehydrogenase complexed with NADP+.
Inagaki E, Ohshima N, Sakamoto K, Babayeva ND, Kato H, Yokoyama S, Tahirov TH
Acta Crystallogr Sect F Struct Biol Cryst Commun 63 462-5 (2007)
PMID: 17554163

Function and Biology Details

Reaction catalysed: 
L-glutamate 5-semialdehyde + NAD(+) + H(2)O = L-glutamate + NADH
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assemblies composition:
homo dimer (preferred)
homo hexamer
Assembly name:
PDBe Complex ID:
PDB-CPX-177922 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
L-glutamate gamma-semialdehyde dehydrogenase Chains: A, B
Molecule details ›
Chains: A, B
Length: 516 amino acids
Theoretical weight: 57.11 KDa
Source organism: Thermus thermophilus HB8
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q5SI02 (Residues: 1-516; Coverage: 100%)
Gene name: TTHA1578
Sequence domains: Aldehyde dehydrogenase family
Structure domains:

Ligands and Environments


Cofactor: Ligand NAP 2 x NAP
3 bound ligands:
Ligand ACT 4 x ACT
Ligand NA 2 x NA
Ligand MPD 7 x MPD
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL44XU
Spacegroup: R3
Unit cell:
a: 102.426Å b: 102.426Å c: 278.837Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.159 0.158 0.18
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

5 citation in other articles

The crystal structure of a ternary complex of betaine aldehyde dehydrogenase from Pseudomonas aeruginosa Provides new insight into the reaction mechanism and shows a novel binding mode of the 2'-phosphate of NADP+ and a novel cation binding site.
González-Segura et al. (2009)
4 more

3 mentions without citation

Structural Biology of Proline Catabolic Enzymes.
Tanner JJ. (2019)
2 more