6lgk

X-ray diffraction
2Å resolution

Crystal structure of an oxido-reductase with mutation

Released:
Source organism: Mus musculus
Entry authors: Yang Y, Lei J, Yin L

Function and Biology Details

Reaction catalysed:
D-glyceraldehyde 3-phosphate + phosphate + NAD(+) = 3-phospho-D-glyceroyl phosphate + NADH
Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
PDBe Complex ID:
PDB-CPX-147820 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glyceraldehyde-3-phosphate dehydrogenase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 333 amino acids
Theoretical weight: 35.84 KDa
Source organism: Mus musculus
Expression system: Escherichia coli K-12
UniProt:
  • Canonical: P16858 (Residues: 1-333; Coverage: 100%)
Gene names: Gapd, Gapdh
Sequence domains:

Ligands and Environments


Cofactor: Ligand NAD 3 x NAD
1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRF BEAMLINE BL19U1
Unit cell:
a: 75.36Å b: 137.17Å c: 141.64Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.146 0.146 0.172
Expression system: Escherichia coli K-12