› 3qlr

X-ray diffraction
2.15Å resolution

Candida albicans dihydrofolate reductase complexed with NADPH and 6-methyl-5-[(3R)-3-(3,4,5-trimethoxyphenyl)pent-1-yn-1-yl]pyrimidine-2,4-diamine (UCP112A)

Released:
DOI: 10.2210/pdb3qlr/pdb
PDB entry 3qlr coloured by chain, front view.
PDB entry 3qlr coloured by chain, side view.
PDB entry 3qlr coloured by chain, top view.
Source organism: Candida albicans
Primary publication:
Crystal structures of Candida albicans dihydrofolate reductase bound to propargyl-linked antifolates reveal the flexibility of active site loop residues critical for ligand potency and selectivity.
Paulsen JL, Bendel SD, Anderson AC
Chem Biol Drug Des 78 505-12 (2011)
PMID: 21726415

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 analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-149838 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Dihydrofolate reductase Chains: A, B
Molecule details ›
Chains: A, B
Length: 192 amino acids
Theoretical weight: 22.19 KDa
Source organism: Candida albicans
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P22906 (Residues: 3-192; Coverage: 99%)
Gene name: DFR1
Sequence domains: Dihydrofolate reductase
Structure domains: Dihydrofolate Reductase, subunit A

Ligands and Environments


Cofactor: Ligand NDP 2 x NDP
3 bound ligands:
Ligand QLR 2 x QLR
Ligand GOL 2 x GOL
Ligand GLY 2 x GLY
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X25
Spacegroup: P21
Unit cell:
a: 37.99Å b: 66.266Å c: 75.888Å
α: 90° β: 92.93° γ: 90°
R-values:
R R work R free
0.179 0.176 0.244
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

6 citation in other articles

Elucidating features that drive the design of selective antifolates using crystal structures of human dihydrofolate reductase.
Lamb et al. (2013)
5 more

2 mentions without citation

Structural analysis of the active sites of dihydrofolate reductase from two species of Candida uncovers ligand-induced conformational changes shared among species.
Paulsen et al. (2013)
1 more