Structure analysis

Crystal structure of the first class MHC mamu and Tat-Tl8 complex

X-ray diffraction
2.8Å resolution
Source organisms:
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: 19362.12 Å2
Buried surface area: 3833.17 Å2
Dissociation area: 1,173.92 Å2
Dissociation energy (ΔGdiss): 5.65 kcal/mol
Dissociation entropy (TΔSdiss): 12.03 kcal/mol
Symmetry number: 1
PDBe Complex ID: PDB-CPX-158315
Assembly 2
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Multimeric state: hetero trimer
Accessible surface area: 19699.44 Å2
Buried surface area: 3735.98 Å2
Dissociation area: 714.78 Å2
Dissociation energy (ΔGdiss): 3.48 kcal/mol
Dissociation entropy (TΔSdiss): 6.91 kcal/mol
Symmetry number: 1
PDBe Complex ID: PDB-CPX-158315

Macromolecules

Chains: B, E
Length: 99 amino acids
Theoretical weight: 11.75 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P61769 (Residues: 21-119; Coverage: 100%)
Gene names: B2M, CDABP0092, HDCMA22P
Pfam: Immunoglobulin C1-set domain
InterPro:
CATH: Immunoglobulins
SCOP: C1 set domains (antibody constant domain-like)

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