Assemblies
Assembly Name:
Interleukin-15 and IG-heavy chain and IG-light lambda chain
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:
Pfam: Interleukin 15
InterPro:
CATH: Interleukin-15/Interleukin-21
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%)
Pfam: Interleukin 15
InterPro:
CATH: Interleukin-15/Interleukin-21

P40933
Chains
Domains
Secondary structure
Flexibility predictions
Early folding residue predictions
Ligand binding sites
Chain: H
Length: 236 amino acids
Theoretical weight: 25.39 KDa
Source organism: Homo sapiens
Expression system: Homo sapiens
Length: 236 amino acids
Theoretical weight: 25.39 KDa
Source organism: Homo sapiens
Expression system: Homo sapiens
- Immunoglobulin-like domain
- Immunoglobulin-like fold
- Immunoglobulin-like domain superfamily
- Immunoglobulin domain subtype
- Immunoglobulin V-set domain
- Immunoglobulin C1-set
- Immunoglobulin/major histocompatibility complex, conserved site
Chain B (auth H)
Domains
Secondary structure
Flexibility predictions
Early folding residue predictions
Ligand binding sites
Chain: L
Length: 211 amino acids
Theoretical weight: 22.92 KDa
Source organism: Homo sapiens
Expression system: Homo sapiens
Length: 211 amino acids
Theoretical weight: 22.92 KDa
Source organism: Homo sapiens
Expression system: Homo sapiens
- Immunoglobulin-like domain
- Immunoglobulin-like fold
- Immunoglobulin-like domain superfamily
- Immunoglobulin domain subtype
- Immunoglobulin V-set domain
- Immunoglobulin C1-set
- Immunoglobulin/major histocompatibility complex, conserved site
Chain C (auth L)
Domains
Secondary structure
Flexibility predictions
Early folding residue predictions
Ligand binding sites