Structure analysis

Crystal Structure of anti-IL-15 Antibody in Complex with human IL-15

X-ray diffraction
2.6Å resolution
Source organism: Homo sapiens
Assembly composition:
hetero trimer (preferred)
Entry contents: 3 distinct polypeptide molecules

Assemblies

Assembly 1 (preferred)
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Multimeric state: hetero trimer
Accessible surface area: 22997.0 Å2
Buried surface area: 6105.05 Å2
Dissociation area: 2,030.91 Å2
Dissociation energy (ΔGdiss): 21.73 kcal/mol
Dissociation entropy (TΔSdiss): 13.5 kcal/mol
Symmetry number: 1
PDBe Complex ID: PDB-CPX-211192

Macromolecules

Chain: A
Length: 114 amino acids
Theoretical weight: 12.78 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P40933 (Residues: 49-162; Coverage: 86%)
Gene name: IL15
Pfam: Interleukin 15
InterPro:
CATH: Interleukin-15/Interleukin-21
PDBe-KB: UniProt Coverage View: P40933  
1114102030405060708090100110
 
50100
UniProt
P40933
Chains
Domains
Secondary structure
Flexibility predictions
Early folding residue predictions
Ligand binding sites

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123620406080100120140160180200220
 
100200
Chains
Chain B (auth H)
Domains
Secondary structure
Flexibility predictions
Early folding residue predictions
Ligand binding sites

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121120406080100120140160180200
 
50100150200
Chains
Chain C (auth L)
Domains
Secondary structure
Flexibility predictions
Early folding residue predictions
Ligand binding sites

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