› 3ddn

X-ray diffraction
2.4Å resolution

Crystal structure of hydroxypyruvic acid phosphate bound D-3-phosphoglycerate dehydrogenase in mycobacterium tuberculosis

Released:
DOI: 10.2210/pdb3ddn/pdb
PDB 3ddn coloured by chain and viewed from the front.
PDB 3ddn coloured by chain and viewed from the side.
PDB 3ddn coloured by chain and viewed from the top.
Source organism: Mycobacterium tuberculosis
Primary publication:
Structural analysis of substrate and effector binding in Mycobacterium tuberculosis D-3-phosphoglycerate dehydrogenase.
Dey S, Burton RL, Grant GA, Sacchettini JC
Biochemistry 47 8271-82 (2008)
PMID: 18627175

Function and Biology Details

Reactions catalysed: 
(R)-2-hydroxyglutarate + NAD(+) = 2-oxoglutarate + NADH
3-phospho-D-glycerate + NAD(+) = 3-phosphonooxypyruvate + NADH
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
D-3-phosphoglycerate dehydrogenase Chains: A, B
Molecule details ›
Chains: A, B
Length: 528 amino acids
Theoretical weight: 54.57 KDa
Source organism: Mycobacterium tuberculosis
Expression system: Escherichia coli
UniProt:
  • Canonical: P9WNX3 (Residues: 2-528; Coverage: 100%)
Gene names: MTV012.10, Rv2996c, serA
Sequence domains:
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand TLA 3 x TLA
Ligand HPV 1 x HPV
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 14-BM-C
Spacegroup: P6522
Unit cell:
a: 165.601Å b: 165.601Å c: 218.299Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.206 0.204 0.244
Expression system: Escherichia coli

Quick links

Citations

2 review citations

D-3-Phosphoglycerate Dehydrogenase.
Grant GA. (2018)
1 more

5 mentions without citation

Contrasting catalytic and allosteric mechanisms for phosphoglycerate dehydrogenases.
Grant GA. (2012)
4 more