Structure analysis

Crystal Structures of the Wild-type, Mutant-P1A and Inactivated Malonate Semialdehyde Decarboxylase: A Structural Basis for the Decarboxylase and Hydratase Activities

X-ray diffraction
1.65Å resolution
Source organism: Pseudomonas pavonaceae
Assembly composition:
homo trimer (preferred)
Entry contents: 1 distinct polypeptide molecule

Assemblies

Assembly 1 (preferred)
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Multimeric state: homo trimer
Accessible surface area: 14232.02 Å2
Buried surface area: 8874.96 Å2
Dissociation area: 4,061.1 Å2
Dissociation energy (ΔGdiss): 43.14 kcal/mol
Dissociation entropy (TΔSdiss): 24.74 kcal/mol
Symmetry number: 3
PDBe Complex ID: PDB-CPX-190201
Assembly 2
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Multimeric state: homo trimer
Accessible surface area: 14047.21 Å2
Buried surface area: 8922.86 Å2
Dissociation area: 4,086.8 Å2
Dissociation energy (ΔGdiss): 45.87 kcal/mol
Dissociation entropy (TΔSdiss): 24.73 kcal/mol
Symmetry number: 3
PDBe Complex ID: PDB-CPX-190201

Macromolecules

Chains: A, B, C, D, E, F
Length: 130 amino acids
Theoretical weight: 14.18 KDa
Source organism: Pseudomonas pavonaceae
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q9EV83 (Residues: 2-130; Coverage: 99%)
Gene name: msaD
Pfam: Tautomerase enzyme
InterPro:
CATH: Macrophage Migration Inhibitory Factor
SCOP: MSAD-like

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