› 1daj

X-ray diffraction
2.3Å resolution

COMPARISON OF TERNARY COMPLEXES OF PNEUMOCYSTIS CARINII AND WILD TYPE HUMAN DIHYDROFOLATE REDUCTASE WITH COENZYME NADPH AND A NOVEL CLASSICAL ANTITUMOR FURO[2,3D]PYRIMIDINE ANTIFOLATE

Released:
DOI: 10.2210/pdb1daj/pdb
PDB entry 1daj coloured by chain, front view.
PDB entry 1daj coloured by chain, side view.
PDB entry 1daj coloured by chain, top view.
Source organism: Pneumocystis carinii
Primary publication:
Comparison of ternary complexes of Pneumocystis carinii and wild-type human dihydrofolate reductase with coenzyme NADPH and a novel classical antitumor furo[2,3-d]pyrimidine antifolate.
Cody V, Galitsky N, Luft JR, Pangborn W, Gangjee A, Devraj R, Queener SF, Blakley RL
Acta Crystallogr D Biol Crystallogr 53 638-49 (1997)
PMID: 15299851

Function and Biology Details

Reaction catalysed: 
5,6,7,8-tetrahydrofolate + NADP(+) = 7,8-dihydrofolate + NADPH
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-147657 (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:
Ligand MOT 1 x MOT
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P21
Unit cell:
a: 37.171Å b: 43.094Å c: 61.049Å
α: 90° β: 94.85° γ: 90°
R-values:
R R work R free
0.181 0.181 not available
Expression system: Escherichia coli

Quick links

Citations

7 citation in other articles

Towards an understanding of drug resistance in malaria: three-dimensional structure of Plasmodium falciparum dihydrofolate reductase by homology building.
Lemcke et al. (1999)
6 more

3 mentions without citation

Utilizing experimental data for reducing ensemble size in flexible-protein docking.
Xu et al. (2012)
2 more