Structure analysis

CL-K1 trimer

X-ray diffraction
2.45Å resolution
Source organism: Homo sapiens
Assembly composition:
homo trimer (preferred)
Entry contents: 1 distinct polypeptide molecule

Assemblies

Assembly 1 (preferred)
Download    3D Visualisation
Multimeric state: homo trimer
Accessible surface area: 23448.62 Å2
Buried surface area: 6457.96 Å2
Dissociation area: 1,210.92 Å2
Dissociation energy (ΔGdiss): 13.37 kcal/mol
Dissociation entropy (TΔSdiss): 12.82 kcal/mol
Symmetry number: 1
PDBe Complex ID: PDB-CPX-189776
Assembly 2
Download    3D Visualisation
Multimeric state: homo trimer
Accessible surface area: 22915.64 Å2
Buried surface area: 6287.54 Å2
Dissociation area: 2,037.54 Å2
Dissociation energy (ΔGdiss): 15.6 kcal/mol
Dissociation entropy (TΔSdiss): 25.22 kcal/mol
Symmetry number: 3
PDBe Complex ID: PDB-CPX-189776

Macromolecules

Chains: A, B, C, D, E, F
Length: 155 amino acids
Theoretical weight: 17.31 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q9BWP8 (Residues: 116-270; Coverage: 63%)
Gene names: COLEC11, UNQ596/PRO1182
Pfam: Lectin C-type domain
InterPro:
CATH: Mannose-Binding Protein A, subunit A

Search similar proteins