› 1evz

X-ray diffraction
2.8Å resolution

CRYSTAL STRUCTURE OF LEISHMANIA MEXICANA GLYCEROL-3-PHOSPHATE DEHYDROGENASE IN COMPLEX WITH NAD

Released:
DOI: 10.2210/pdb1evz/pdb
PDB entry 1evz coloured by chain, front view.
PDB entry 1evz coloured by chain, side view.
PDB entry 1evz coloured by chain, top view.
Source organism: Leishmania mexicana
Primary publication:
A potential target enzyme for trypanocidal drugs revealed by the crystal structure of NAD-dependent glycerol-3-phosphate dehydrogenase from Leishmania mexicana.
Suresh S, Turley S, Opperdoes FR, Michels PA, Hol WG
Structure 8 541-52 (2000)
PMID: 10801498

Function and Biology Details

Reaction catalysed: 
sn-glycerol 3-phosphate + NAD(+) = glycerone phosphate + NADH
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-161036 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glycerol-3-phosphate dehydrogenase [NAD(+)], glycosomal Chain: A
Molecule details ›
Chain: A
Length: 366 amino acids
Theoretical weight: 39.32 KDa
Source organism: Leishmania mexicana
Expression system: Escherichia coli
UniProt:
  • Canonical: P90551 (Residues: 1-366; Coverage: 100%)
Gene name: GPD
Sequence domains:
Structure domains:

Ligands and Environments


Cofactor: Ligand NAD 1 x NAD
1 bound ligand:
Ligand MYS 1 x MYS
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL7-1
Spacegroup: P41212
Unit cell:
a: 69.85Å b: 69.85Å c: 211.88Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.183 0.183 0.255
Expression system: Escherichia coli

Quick links

Citations

3 review citations

Evolution of protein fold in the presence of functional constraints.
Andreeva et al. (2006)
2 more

3 mentions without citation

The Potential of Secondary Metabolites from Plants as Drugs or Leads against Protozoan Neglected Diseases-Part III: In-Silico Molecular Docking Investigations.
Ogungbe et al. (2016)
2 more