3cif

X-ray diffraction
2Å resolution

Crystal Structure of C153S mutant glyceraldehyde 3-phosphate dehydrogenase from Cryptosporidium parvum

Released:

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

Assemblies composition:
homo tetramer
homo dimer (preferred)
PDBe Complex ID:
PDB-CPX-182225 (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: 359 amino acids
Theoretical weight: 38.28 KDa
Source organism: Cryptosporidium parvum
Expression system: Escherichia coli
UniProt:
  • Canonical: Q7YYQ9 (Residues: 1-339; Coverage: 100%)
Gene names: 1MB.519, CPATCC_002941, cgd6_3790
Sequence domains:
Structure domains:

Ligands and Environments


Cofactor: Ligand NAD 4 x NAD
3 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 22-ID
Spacegroup: P21
Unit cell:
a: 68Å b: 120.1Å c: 79.28Å
α: 90° β: 92.08° γ: 90°
R-values:
R R work R free
0.179 0.178 0.21
Expression system: Escherichia coli