1dyr

X-ray diffraction
1.86Å resolution

THE STRUCTURE OF PNEUMOCYSTIS CARINII DIHYDROFOLATE REDUCTASE TO 1.9 ANGSTROMS RESOLUTION

Released:

Function and Biology Details

Reaction catalysed:
5,6,7,8-tetrahydrofolate + NADP(+) = 7,8-dihydrofolate + NADPH
Biochemical function:
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Dihydrofolate reductase Chain: A
Molecule details ›
Chain: A
Length: 206 amino acids
Theoretical weight: 23.92 KDa
Source organism: Pneumocystis carinii
Expression system: Escherichia coli
UniProt:
  • Canonical: P16184 (Residues: 1-206; Coverage: 100%)
Sequence domains: Dihydrofolate reductase
Structure domains: Dihydrofolate Reductase, subunit A

Ligands and Environments


Cofactor: Ligand NDP 1 x NDP
1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P21
Unit cell:
a: 69.9Å b: 43.6Å c: 37.6Å
α: 90° β: 117.7° γ: 90°
R-values:
R R work R free
0.181 not available not available
Expression system: Escherichia coli