Structure analysis

ENGINEERING A MISFOLDED FORM OF CD2

X-ray diffraction
3.1Å resolution
Source organism: Rattus norvegicus
Assemblies composition:
homo tetramer
homo dimer (preferred)
Entry contents: 1 distinct polypeptide molecule

Assemblies

Assembly 1
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Multimeric state: homo tetramer
Accessible surface area: 18675.43 Å2
Buried surface area: 16544.05 Å2
Dissociation area: 1,105.12 Å2
Dissociation energy (ΔGdiss): -7.88 kcal/mol
Dissociation entropy (TΔSdiss): 12.61 kcal/mol
Symmetry number: 4
PDBe Complex ID: PDB-CPX-140436
Assembly 2 (preferred)
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Multimeric state: homo dimer
Accessible surface area: 10425.93 Å2
Buried surface area: 7183.12 Å2
Dissociation area: 3,591.56 Å2
Dissociation energy (ΔGdiss): 55.25 kcal/mol
Dissociation entropy (TΔSdiss): 12.57 kcal/mol
Symmetry number: 2
PDBe Complex ID: PDB-CPX-140435
Assembly 3
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Multimeric state: homo dimer
Accessible surface area: 10420.35 Å2
Buried surface area: 7190.08 Å2
Dissociation area: 3,595.04 Å2
Dissociation energy (ΔGdiss): 55.31 kcal/mol
Dissociation entropy (TΔSdiss): 12.57 kcal/mol
Symmetry number: 2
PDBe Complex ID: PDB-CPX-140435

Macromolecules

Chains: A, B, C, D
Length: 97 amino acids
Theoretical weight: 10.9 KDa
Source organism: Rattus norvegicus
Expression system: Escherichia coli
UniProt:
  • Canonical: P08921 (Residues: 23-121; Coverage: 30%)
Gene name: Cd2
Pfam: Immunoglobulin V-set domain
InterPro:
CATH: Immunoglobulins
SCOP: V set domains (antibody variable domain-like)

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