Structure analysis

Crystal structure of 2A protease from Human rhinovirus C15

X-ray diffraction
2.602Å resolution
Source organism: Rhinovirus C
Assembly composition:
monomeric (preferred)
Entry contents: 1 distinct polypeptide molecule

Assemblies

Assembly 1 (preferred)
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Multimeric state: monomeric
Accessible surface area: 7412.47 Å2
Buried surface area: 0.0 Å2
Dissociation area: 0 Å2
Dissociation energy (ΔGdiss): 0 kcal/mol
Dissociation entropy (TΔSdiss): 0 kcal/mol
Symmetry number: 1
PDBe Complex ID: PDB-CPX-122966
Assembly 2
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Multimeric state: monomeric
Accessible surface area: 7541.77 Å2
Buried surface area: 0.0 Å2
Dissociation area: 0 Å2
Dissociation energy (ΔGdiss): 0 kcal/mol
Dissociation entropy (TΔSdiss): 0 kcal/mol
Symmetry number: 1
PDBe Complex ID: PDB-CPX-122966
Assembly 3
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Multimeric state: monomeric
Accessible surface area: 7556.16 Å2
Buried surface area: 0.0 Å2
Dissociation area: 0 Å2
Dissociation energy (ΔGdiss): 0 kcal/mol
Dissociation entropy (TΔSdiss): 0 kcal/mol
Symmetry number: 1
PDBe Complex ID: PDB-CPX-122966
Assembly 4
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Multimeric state: monomeric
Accessible surface area: 7441.3 Å2
Buried surface area: 0.0 Å2
Dissociation area: 0 Å2
Dissociation energy (ΔGdiss): 0 kcal/mol
Dissociation entropy (TΔSdiss): 0 kcal/mol
Symmetry number: 1
PDBe Complex ID: PDB-CPX-122966

Macromolecules

Chains: A, B, C, D
Length: 139 amino acids
Theoretical weight: 15.24 KDa
Source organism: Rhinovirus C
Expression system: Escherichia coli
UniProt:
  • Canonical: E5D8F2 (Residues: 847-983; Coverage: 6%)
Pfam: Picornavirus core protein 2A
InterPro:
CATH: Trypsin-like serine proteases

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