Structure analysis

E. coli Quinol fumarate reductase FrdA E245Q mutation

X-ray diffraction
4.223Å resolution
Assembly composition:
hetero tetramer (preferred)
Entry contents: 4 distinct polypeptide molecules

Assemblies

Assembly 1 (preferred)
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Multimeric state: hetero tetramer
Accessible surface area: 39772.03 Å2
Buried surface area: 17143.01 Å2
Dissociation area: 3,210.06 Å2
Dissociation energy (ΔGdiss): 55.13 kcal/mol
Dissociation entropy (TΔSdiss): 13.23 kcal/mol
Symmetry number: 1
PDBe Complex ID: PDB-CPX-132435
Complex Portal ID: CPX-1967
Assembly 2
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Multimeric state: hetero tetramer
Accessible surface area: 40131.87 Å2
Buried surface area: 16962.56 Å2
Dissociation area: 3,223.56 Å2
Dissociation energy (ΔGdiss): 56.45 kcal/mol
Dissociation entropy (TΔSdiss): 13.24 kcal/mol
Symmetry number: 1
PDBe Complex ID: PDB-CPX-132435
Complex Portal ID: CPX-1967

Macromolecules

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Chains: C, G
Length: 130 amino acids
Theoretical weight: 14.9 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli
UniProt:
  • Canonical: P0A8Q0 (Residues: 2-131; Coverage: 99%)
Gene names: JW4113, b4152, frdC
Pfam: Fumarate reductase subunit C
InterPro:

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Chains: D, H
Length: 119 amino acids
Theoretical weight: 13.12 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli
UniProt:
  • Canonical: P0A8Q3 (Residues: 1-119; Coverage: 100%)
Gene names: JW4112, b4151, frdD
Pfam: Fumarate reductase subunit D
InterPro:

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