Assemblies
Multimeric state:
hetero trimer
Accessible surface area:
18639.15 Å2
Buried surface area:
4414.32 Å2
Dissociation area:
1,314.91
Å2
Dissociation energy (ΔGdiss):
3.55
kcal/mol
Dissociation entropy (TΔSdiss):
12.05
kcal/mol
Symmetry number:
1
PDBe Complex ID:
PDB-CPX-134989
Macromolecules
Chain: A
Length: 272 amino acids
Theoretical weight: 31.52 KDa
Source organism: Mus musculus
Expression system: Escherichia coli
UniProt:
Pfam:
InterPro:
SCOP:
Length: 272 amino acids
Theoretical weight: 31.52 KDa
Source organism: Mus musculus
Expression system: Escherichia coli
UniProt:
- Canonical: P01899 (Residues: 25-296; Coverage: 81%)
Pfam:
InterPro:
- MHC class I-like antigen recognition-like superfamily
- MHC class I-like antigen recognition-like
- MHC classes I/II-like antigen recognition protein
- MHC class I alpha chain, alpha1 alpha2 domains
- Immunoglobulin-like fold
- Immunoglobulin-like domain
- Immunoglobulin-like domain superfamily
- Immunoglobulin C1-set
- Immunoglobulin/major histocompatibility complex, conserved site
SCOP:
PDBe-KB: UniProt Coverage View:
P01899
P01899
Chains
Domains
Secondary structure
Flexibility predictions
Early folding residue predictions
Interaction interfaces
Chain: B
Length: 99 amino acids
Theoretical weight: 11.7 KDa
Source organism: Mus musculus
Expression system: Escherichia coli
UniProt:
Pfam: Immunoglobulin C1-set domain
InterPro:
SCOP: C1 set domains (antibody constant domain-like)
Length: 99 amino acids
Theoretical weight: 11.7 KDa
Source organism: Mus musculus
Expression system: Escherichia coli
UniProt:
- Canonical: P01887 (Residues: 21-119; Coverage: 100%)
Pfam: Immunoglobulin C1-set domain
InterPro:
- Immunoglobulin-like fold
- Immunoglobulin-like domain
- Immunoglobulin-like domain superfamily
- Immunoglobulin C1-set
- Immunoglobulin/major histocompatibility complex, conserved site
- Beta-2-Microglobulin
SCOP: C1 set domains (antibody constant domain-like)
PDBe-KB: UniProt Coverage View:
P01887
P01887
Chains
Domains
Secondary structure
Flexibility predictions
Early folding residue predictions
Interaction interfaces
Sequence conservation