› 1hfp

X-ray diffraction
2.1Å resolution

COMPARISON OF TERNARY CRYSTAL COMPLEXES OF HUMAN DIHYDROFOLATE REDUCTASE WITH NADPH AND A CLASSICAL ANTITUMOR FUROPYRIMDINE

Released:
DOI: 10.2210/pdb1hfp/pdb
PDB entry 1hfp coloured by chain, front view.
PDB entry 1hfp coloured by chain, side view.
PDB entry 1hfp coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Comparison of ternary crystal complexes of F31 variants of human dihydrofolate reductase with NADPH and a classical antitumor furopyrimidine.
Cody V, Galitsky N, Luft JR, Pangborn W, Blakley RL, Gangjee A
Anticancer Drug Des 13 307-15 (1998)
PMID: 9627670

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-132447 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Dihydrofolate reductase Chain: A
Molecule details ›
Chain: A
Length: 186 amino acids
Theoretical weight: 21.26 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
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 1 x NDP
1 bound ligand:
Ligand MOT 1 x MOT
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: R3
Unit cell:
a: 87.12Å b: 87.12Å c: 77.014Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.181 0.181 not available
Expression system: Escherichia coli

Quick links

Citations

12 citation in other articles

Insights into antifolate resistance from malarial DHFR-TS structures.
Yuvaniyama et al. (2003)
11 more

5 mentions without citation

Dehydron: a structurally encoded signal for protein interaction.
Fernández et al. (2003)
4 more