1dc3

X-ray diffraction
2.5Å resolution

STRUCTURAL ANALYSIS OF GLYCERALDEHYDE 3-PHOSPHATE DEHYDROGENASE FROM ESCHERICHIA COLI: DIRECT EVIDENCE FOR SUBSTRATE BINDING AND COFACTOR-INDUCED CONFORMATIONAL CHANGES

Released:

Function and Biology Details

Structure analysis Details

Assemblies composition:
homo dimer (preferred)
homo tetramer
PDBe Complex ID:
PDB-CPX-141861 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glyceraldehyde-3-phosphate dehydrogenase A Chains: A, B
Molecule details ›
Chains: A, B
Length: 330 amino acids
Theoretical weight: 35.45 KDa
Source organism: Escherichia coli
UniProt:
  • Canonical: P0A9B2 (Residues: 2-331; Coverage: 100%)
Gene names: JW1768, b1779, gapA
Sequence domains:
Structure domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X9B
Spacegroup: I41
Unit cell:
a: 119.57Å b: 119.57Å c: 158.55Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.189 0.189 0.241