Structure analysis

Bifunctional dCTP deaminase-dUTPase mutant enzyme variant E145A from Methanocaldococcus jannaschii in complex with alpha,beta-imido dUTP and magnesium

X-ray diffraction
2.3Å resolution
Assemblies composition:
homo trimer (preferred)
homo hexamer
homo 24-mer
Entry contents: 1 distinct polypeptide molecule

Assemblies

Assembly 1 (preferred)
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Multimeric state: homo trimer
Accessible surface area: 21192.21 Å2
Buried surface area: 14789.48 Å2
Dissociation area: 6,727.3 Å2
Dissociation energy (ΔGdiss): 82.12 kcal/mol
Dissociation entropy (TΔSdiss): 27.46 kcal/mol
Symmetry number: 3
PDBe Complex ID: PDB-CPX-176493
Assembly 2
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Multimeric state: homo hexamer
Accessible surface area: 39563.64 Å2
Buried surface area: 32404.61 Å2
Dissociation area: 1,581.8 Å2
Dissociation energy (ΔGdiss): 9.04 kcal/mol
Dissociation entropy (TΔSdiss): 14.4 kcal/mol
Symmetry number: 6
PDBe Complex ID: PDB-CPX-176494
Assembly 3
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Multimeric state: homo 24-mer
Accessible surface area: 148589.1 Å2
Buried surface area: 139271.2 Å2
Dissociation area: 10,494.51 Å2
Dissociation energy (ΔGdiss): -97.39 kcal/mol
Dissociation entropy (TΔSdiss): 106.42 kcal/mol
Symmetry number: 24
PDBe Complex ID: PDB-CPX-176492

Macromolecules

Chain: A
Length: 204 amino acids
Theoretical weight: 23.4 KDa
Source organism: Methanocaldococcus jannaschii
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q57872 (Residues: 1-204; Coverage: 100%)
Gene names: MJ0430, dcd
Pfam: dCTP deaminase-like
InterPro:
CATH: Deoxyuridine 5'-Triphosphate Nucleotidohydrolase; Chain A

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