› 1mvt

X-ray diffraction
1.8Å resolution

Analysis of Two Polymorphic Forms of a Pyrido[2,3-d]pyrimidine N9-C10 Reverse-Bridge Antifolate Binary Complex with Human Dihydrofolate Reductase

Released:
DOI: 10.2210/pdb1mvt/pdb
PDB entry 1mvt coloured by chain, front view.
PDB entry 1mvt coloured by chain, side view.
PDB entry 1mvt coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Analysis of two polymorphic forms of a pyrido[2,3-d]pyrimidine N9-C10 reversed-bridge antifolate binary complex with human dihydrofolate reductase.
Cody V, Galitsky N, Luft JR, Pangborn W, Gangjee A
Acta Crystallogr D Biol Crystallogr 59 654-61 (2003)
PMID: 12657784

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: 187 amino acids
Theoretical weight: 21.48 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P00374 (Residues: 1-187; Coverage: 100%)
Gene name: DHFR
Sequence domains: Dihydrofolate reductase
Structure domains: Dihydrofolate Reductase, subunit A

Ligands and Environments

2 bound ligands:
Ligand SO4 2 x SO4
Ligand DTM 1 x DTM
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: R3
Unit cell:
a: 106.78Å b: 106.78Å c: 43.82Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.216 0.194 not available
Expression system: Escherichia coli

Quick links

Citations

3 citation in other articles

Increasing methotrexate resistance by combination of active-site mutations in human dihydrofolate reductase.
Volpato et al. (2007)
2 more

3 mentions without citation

Pharmacophore-based virtual screening versus docking-based virtual screening: a benchmark comparison against eight targets.
Chen et al. (2009)
2 more