Structure analysis

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

X-ray diffraction
1.84Å resolution
Source organism: Homo sapiens
Assembly composition:
monomeric (preferred)
Entry contents: 1 distinct polypeptide molecule

Assemblies

Assembly 1
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Multimeric state: monomeric
Accessible surface area: 9700 Å2
Buried surface area: 3200 Å2
Dissociation area: 100 Å2
Dissociation energy (ΔGdiss): 0 kcal/mol
Dissociation entropy (TΔSdiss): -1 kcal/mol
Interface energy (ΔGint): -68 kcal/mol
Symmetry number: 1
Assembly 2 (preferred)
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Multimeric state: monomeric
Accessible surface area: 9800 Å2
Buried surface area: 3700 Å2
Dissociation area: 50 Å2
Dissociation energy (ΔGdiss): 1 kcal/mol
Dissociation entropy (TΔSdiss): -1 kcal/mol
Interface energy (ΔGint): -110 kcal/mol
Symmetry number: 1

Macromolecules

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
Pfam: Dihydrofolate reductase
InterPro:
CATH: Dihydrofolate Reductase, subunit A

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