PDBe 1cer

X-ray diffraction
2.5Å resolution

DETERMINANTS OF ENZYME THERMOSTABILITY OBSERVED IN THE MOLECULAR STRUCTURE OF THERMUS AQUATICUS D-GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE AT 2.5 ANGSTROMS RESOLUTION

Released:

Function and Biology Details

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glyceraldehyde-3-phosphate dehydrogenase Chains: A, B, C, D, O, P, Q, R
Molecule details ›
Chains: A, B, C, D, O, P, Q, R
Length: 331 amino acids
Theoretical weight: 35.94 KDa
Source organism: Thermus aquaticus
Expression system: Escherichia coli
UniProt:
  • Canonical: P00361 (Residues: 1-331; Coverage: 100%)
Gene name: gap
Sequence domains:
Structure domains:

Ligands and Environments


Cofactor: Ligand NAD 8 x NAD
No bound ligands

No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P212121
Unit cell:
a: 144.77Å b: 148.77Å c: 149.5Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.205 0.205 not available
Expression system: Escherichia coli