› 3roa

X-ray diffraction
2.3Å resolution

Candida glabrata dihydrofolate reductase complexed with NADPH and 6-ethyl-5-[(3R)-3-[3-methoxy-5-(morpholin-4-yl)phenyl]but-1-yn-1-yl]pyrimidine-2,4-diamine (UCP1004)

Released:
DOI: 10.2210/pdb3roa/pdb
PDB entry 3roa coloured by chain, front view.
PDB entry 3roa coloured by chain, side view.
PDB entry 3roa coloured by chain, top view.
Source organism: [Candida] glabrata
Primary publication:
Structural analysis of the active sites of dihydrofolate reductase from two species of Candida uncovers ligand-induced conformational changes shared among species.
Paulsen JL, Viswanathan K, Wright DL, Anderson AC
Bioorg Med Chem Lett 23 1279-84 (2013)
PMID: 23375226

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-179620 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Dihydrofolate reductase Chains: A, B
Molecule details ›
Chains: A, B
Length: 225 amino acids
Theoretical weight: 26.21 KDa
Source organism: [Candida] glabrata
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q6FPH0 (Residues: 3-217; Coverage: 99%)
Gene name: CAGL0J03894g
Sequence domains: Dihydrofolate reductase
Structure domains: Dihydrofolate Reductase, subunit A

Ligands and Environments


Cofactor: Ligand NDP 2 x NDP
2 bound ligands:
Ligand 06V 2 x 06V
Ligand CL 2 x CL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X25
Spacegroup: P41
Unit cell:
a: 42.71Å b: 42.71Å c: 229.47Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.207 0.204 0.258
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

1 review citation

Antifolate agents: a patent review (2010 - 2013).
Anderson et al. (2014)
8 other articles

1 mention 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)