Structure analysis

Lon protease proteolytic domain complexed with covalent boronic acid inhibitor

X-ray diffraction
3.51Å resolution
Source organism: Homo sapiens
Assembly composition:
monomeric (preferred)
Entry contents: 1 distinct polypeptide molecule

Assemblies

Assembly 1 (preferred)
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Multimeric state: monomeric
Accessible surface area: 9439.22 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-153219
Assembly 2
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Multimeric state: monomeric
Accessible surface area: 8835.52 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-153219
Assembly 3
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Multimeric state: monomeric
Accessible surface area: 9667.55 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-153219

Macromolecules

Chains: A, B, C
Length: 218 amino acids
Theoretical weight: 23.79 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P36776 (Residues: 754-959; Coverage: 22%)
Gene names: LONP1, PRSS15
Pfam: Lon protease (S16) C-terminal proteolytic domain
InterPro:

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