› 2bhq

X-ray diffraction
1.4Å resolution

Crystal Analysis of 1-Pyrroline-5-Carboxylate Dehydrogenase from Thermus with bound product glutamate.

Released:
DOI: 10.2210/pdb2bhq/pdb
PDB entry 2bhq coloured by chain, front view.
PDB entry 2bhq coloured by chain, side view.
PDB entry 2bhq coloured by chain, top view.
Source organism: Thermus thermophilus HB8
Primary publication:
Crystal structure of Thermus thermophilus Delta1-pyrroline-5-carboxylate dehydrogenase.
Inagaki E, Ohshima N, Takahashi H, Kuroishi C, Yokoyama S, Tahirov TH
J Mol Biol 362 490-501 (2006)
PMID: 16934832

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

Assembly composition:
homo hexamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-177924 (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

4 bound ligands:
Ligand GLU 2 x GLU
Ligand MRD 5 x MRD
Ligand MPD 4 x MPD
Ligand ACT 2 x ACT
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL26B1
Spacegroup: R3
Unit cell:
a: 102.618Å b: 102.618Å c: 279.074Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.17 0.17 0.186
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

5 review citations

Structural biology of proline catabolism.
Tanner JJ. (2008)
4 more

5 mentions without citation

Insights into Aldehyde Dehydrogenase Enzymes: A Structural Perspective.
Shortall et al. (2021)
4 more