Structure analysis

Structure of a dihydropteroate synthase (folP) in complex with pteroic acid from Coxiella burnetii

X-ray diffraction
1.895Å resolution
Source organism: Coxiella burnetii
Assemblies composition:
homo tetramer
homo dimer (preferred)
Entry contents: 1 distinct polypeptide molecule

Assemblies

Assembly 1
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Multimeric state: homo tetramer
Accessible surface area: 45350.11 Å2
Buried surface area: 6072.55 Å2
Dissociation area: 1,294.94 Å2
Dissociation energy (ΔGdiss): -26.92 kcal/mol
Dissociation entropy (TΔSdiss): 39.74 kcal/mol
Symmetry number: 1
PDBe Complex ID: PDB-CPX-182914
Assembly 2 (preferred)
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Multimeric state: homo dimer
Accessible surface area: 21090.47 Å2
Buried surface area: 4738.76 Å2
Dissociation area: 1,413.11 Å2
Dissociation energy (ΔGdiss): 17.1 kcal/mol
Dissociation entropy (TΔSdiss): 13.25 kcal/mol
Symmetry number: 2
PDBe Complex ID: PDB-CPX-182913
Assembly 3
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Multimeric state: homo dimer
Accessible surface area: 21159.14 Å2
Buried surface area: 4442.24 Å2
Dissociation area: 1,437.3 Å2
Dissociation energy (ΔGdiss): 16.15 kcal/mol
Dissociation entropy (TΔSdiss): 13.26 kcal/mol
Symmetry number: 2
PDBe Complex ID: PDB-CPX-182913

Macromolecules

Chains: A, B, C, D
Length: 314 amino acids
Theoretical weight: 35.88 KDa
Source organism: Coxiella burnetii
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q83BY6 (Residues: 1-297; Coverage: 100%)
Gene names: CBU_1351, folP
Pfam: Pterin binding enzyme
InterPro:
CATH: Dihydropteroate synthase-like

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