› 3gpd

X-ray diffraction
3.5Å resolution

TWINNING IN CRYSTALS OF HUMAN SKELETAL MUSCLE D-GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE

Released:
DOI: 10.2210/pdb3gpd/pdb
PDB entry 3gpd coloured by chain, front view.
PDB entry 3gpd coloured by chain, side view.
PDB entry 3gpd coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Twinning in crystals of human skeletal muscle D-glyceraldehyde-3-phosphate dehydrogenase.
Mercer WD, Winn SI, Watson HC
J Mol Biol 104 277-83 (1976)
PMID: 957435

Function and Biology Details

Reaction catalysed: 
D-glyceraldehyde 3-phosphate + phosphate + NAD(+) = 3-phospho-D-glyceroyl phosphate + 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-137626 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glyceraldehyde-3-phosphate dehydrogenase Chains: G, R
Molecule details ›
Chains: G, R
Length: 334 amino acids
Theoretical weight: 35.92 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: P04406 (Residues: 2-335; Coverage: 100%)
Gene names: CDABP0047, GAPD, GAPDH, OK/SW-cl.12
Sequence domains:
Structure domains:

Ligands and Environments


Cofactor: Ligand NAD 2 x NAD
1 bound ligand:
Ligand SO4 4 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: C2
Unit cell:
a: 132.4Å b: 97.9Å c: 81.6Å
α: 90° β: 114.3° γ: 90°
R-values:
R R work R free
0.33 0.33 not available
Expression system: Not provided

Quick links

Citations

5 review citations

Molecular mechanisms and potential clinical significance of S-glutathionylation.
Dalle-Donne et al. (2008)
4 more

8 mentions without citation

Conserved and host-specific features of influenza virion architecture.
Hutchinson et al. (2014)
7 more