› 2p9c

X-ray diffraction
2.46Å resolution

Crystal structure of serine bound G336V mutant of E.coli phosphoglycerate dehydrogenase

Released:
DOI: 10.2210/pdb2p9c/pdb
PDB entry 2p9c coloured by chain, front view.
PDB entry 2p9c coloured by chain, side view.
PDB entry 2p9c coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
The effect of hinge mutations on effector binding and domain rotation in Escherichia coli D-3-phosphoglycerate dehydrogenase.
Dey S, Hu Z, Xu XL, Sacchettini JC, Grant GA
J Biol Chem 282 18418-18426 (2007)
PMID: 17459882

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 domains:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-141925 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
D-3-phosphoglycerate dehydrogenase Chains: A, B
Molecule details ›
Chains: A, B
Length: 410 amino acids
Theoretical weight: 44.14 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P0A9T0 (Residues: 1-410; Coverage: 100%)
Gene names: JW2880, b2913, serA
Sequence domains:
Structure domains:

Ligands and Environments


Cofactor: Ligand NAI 2 x NAI
1 bound ligand:
Ligand SER 2 x SER
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: OTHER
Spacegroup: P21212
Unit cell:
a: 142.142Å b: 130.785Å c: 50.188Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.222 0.219 0.281
Expression system: Escherichia coli

Quick links

Citations

2 review citations

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

1 mention without citation

Insight into de-regulation of amino acid feedback inhibition: a focus on structure analysis method.
Naz et al. (2023)