Structure analysis

STRUCTURE OF THE FMDV LEADER PROTEASE

X-ray diffraction
3Å resolution
Assembly composition:
homo dimer (preferred)
Entry contents: 1 distinct polypeptide molecule

Assemblies

Assembly 1
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Multimeric state: homo dimer
Accessible surface area: 15138.77 Å2
Buried surface area: 3162.87 Å2
Dissociation area: 1,510.44 Å2
Dissociation energy (ΔGdiss): 7.13 kcal/mol
Dissociation entropy (TΔSdiss): 12.05 kcal/mol
Symmetry number: 1
PDBe Complex ID: PDB-CPX-136753
Assembly 2 (preferred)
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Multimeric state: homo dimer
Accessible surface area: 15143.04 Å2
Buried surface area: 3388.57 Å2
Dissociation area: 1,512.62 Å2
Dissociation energy (ΔGdiss): 7.26 kcal/mol
Dissociation entropy (TΔSdiss): 12.06 kcal/mol
Symmetry number: 1
PDBe Complex ID: PDB-CPX-136753
Assembly 3
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Multimeric state: homo dimer
Accessible surface area: 15187.61 Å2
Buried surface area: 3079.84 Å2
Dissociation area: 1,465.86 Å2
Dissociation energy (ΔGdiss): 7.22 kcal/mol
Dissociation entropy (TΔSdiss): 12.04 kcal/mol
Symmetry number: 1
PDBe Complex ID: PDB-CPX-136753
Assembly 4
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Multimeric state: homo dimer
Accessible surface area: 15103.31 Å2
Buried surface area: 2946.59 Å2
Dissociation area: 1,417.52 Å2
Dissociation energy (ΔGdiss): 8.76 kcal/mol
Dissociation entropy (TΔSdiss): 12.03 kcal/mol
Symmetry number: 1
PDBe Complex ID: PDB-CPX-136753

Macromolecules

Chains: A, B, C, D, E, F, G, H
Length: 173 amino acids
Theoretical weight: 19.78 KDa
Source organism: Foot-and-mouth disease virus (strain O1)
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P03305 (Residues: 29-201; Coverage: 7%)
Pfam: Foot-and-mouth virus L-proteinase
InterPro:
CATH: Cysteine proteinases
SCOP: FMDV leader protease

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