3f8z

X-ray diffraction
2.01Å resolution

Human Dihydrofolate Reductase Structural Data with Active Site Mutant Enzyme Complexes

Released:

Function and Biology Details

Reaction catalysed:
5,6,7,8-tetrahydrofolate + NADP(+) = 7,8-dihydrofolate + NADPH
Biochemical function:
Cellular component:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Dihydrofolate reductase Chain: A
Molecule details ›
Chain: A
Length: 187 amino acids
Theoretical weight: 21.41 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P00374 (Residues: 1-187; Coverage: 100%)
  • Best match: P00374-2 (Residues: 1-135)
Gene name: DHFR
Sequence domains: Dihydrofolate reductase
Structure domains: Dihydrofolate Reductase, subunit A

Ligands and Environments


Cofactor: Ligand NDP 1 x NDP
2 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU300
Spacegroup: R3
Unit cell:
a: 84.416Å b: 84.416Å c: 77.934Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.164 0.161 0.219
Expression system: Escherichia coli