› 4kd7

X-ray diffraction
2.72Å resolution

Human dihydrofolate reductase complexed with NADPH and 5-{3-[3-methoxy-5(pyridine-4-yl)phenyl]prop-1-yn-1-yl}-6-ethyl-pyrimidine-2,4-diamine

Released:
DOI: 10.2210/pdb4kd7/pdb
PDB entry 4kd7 coloured by chain, front view.
PDB entry 4kd7 coloured by chain, side view.
PDB entry 4kd7 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Elucidating features that drive the design of selective antifolates using crystal structures of human dihydrofolate reductase.
Lamb KM, G-Dayanandan N, Wright DL, Anderson AC
Biochemistry 52 7318-26 (2013)
PMID: 24053334

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-132447 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Dihydrofolate reductase Chains: A, B
Molecule details ›
Chains: A, B
Length: 186 amino acids
Theoretical weight: 21.35 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P00374 (Residues: 2-187; Coverage: 100%)
Gene name: DHFR
Sequence domains: Dihydrofolate reductase
Structure domains: Dihydrofolate Reductase, subunit A

Ligands and Environments


Cofactor: Ligand NDP 2 x NDP
2 bound ligands:
Ligand 9DR 2 x 9DR
Ligand SO4 4 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X4A
Spacegroup: C2221
Unit cell:
a: 105.258Å b: 105.249Å c: 144.684Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.177 0.174 0.22
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

16 citation in other articles

Multistage and transmission-blocking targeted antimalarials discovered from the open-source MMV Pandemic Response Box.
Reader et al. (2021)
15 more

5 mentions without citation

A benchmark driven guide to binding site comparison: An exhaustive evaluation using tailor-made data sets (ProSPECCTs).
Ehrt et al. (2018)
4 more