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Structural Analysis of Pneumocystis carinii and Human DHFR Complexes with NADPH and a Series of Five Potent 5-(omega-carboxy(alkyloxy)pyrido[2,3-d]pyridine Derivativea

X-ray diffraction
2Å resolution
PDB entry 3nzc coloured by chain, front view.
PDB entry 3nzc coloured by chain, side view.
PDB entry 3nzc coloured by chain, top view.
Source organism: Pneumocystis carinii
Assembly composition:
monomeric (preferred)
Entry contents: 1 distinct polypeptide molecule

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Assemblies

Assembly 1 (preferred)
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Assembly Name: Dihydrofolate reductase
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Multimeric state: monomeric
Accessible surface area: 10796.96 Å2
Buried surface area: 705.17 Å2
Dissociation area: 103.54 Å2
Dissociation energy (ΔGdiss): 0.06 kcal/mol
Dissociation entropy (TΔSdiss): 1.07 kcal/mol
Symmetry number: 1
PDBe Complex ID: PDB-CPX-147657

Macromolecules

Dihydrofolate reductase
Chain: X
Length: 206 amino acids
Theoretical weight: 23.92 KDa
Source organism: Pneumocystis carinii
Expression system: Escherichia coli
UniProt:
  • Canonical: P16184 (Residues: 1-206; Coverage: 100%)
Pfam: Dihydrofolate reductase
InterPro:
CATH: Dihydrofolate Reductase, subunit A
Dihydrofolate reductase in PDB entry 3nzc, assembly 1, front view.
Dihydrofolate reductase in PDB entry 3nzc, assembly 1, side view.
Dihydrofolate reductase in PDB entry 3nzc, assembly 1, top view.
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