Structure analysis

The structure of the complex between complement receptor CR2 and its ligand complement fragment C3d

X-ray diffraction
3.16Å resolution
Source organism: Homo sapiens
Assembly composition:
hetero dimer (preferred)
Entry contents: 2 distinct polypeptide molecules

Assemblies

Assembly 1 (preferred)
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Multimeric state: hetero dimer
Accessible surface area: 18259.22 Å2
Buried surface area: 2241.21 Å2
Dissociation area: 1,120.61 Å2
Dissociation energy (ΔGdiss): -6.45 kcal/mol
Dissociation entropy (TΔSdiss): 12.3 kcal/mol
Symmetry number: 1
PDBe Complex ID: PDB-CPX-133844
Assembly 2
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Multimeric state: hetero dimer
Accessible surface area: 18569.21 Å2
Buried surface area: 2150.16 Å2
Dissociation area: 1,075.08 Å2
Dissociation energy (ΔGdiss): -6.22 kcal/mol
Dissociation entropy (TΔSdiss): 12.3 kcal/mol
Symmetry number: 1
PDBe Complex ID: PDB-CPX-133844

Macromolecules

Chains: A, B
Length: 310 amino acids
Theoretical weight: 34.75 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: P01024 (Residues: 996-1303; Coverage: 19%)
Gene names: C3, CPAMD1
Pfam: A-macroglobulin TED domain
InterPro:
CATH: Glycosyltransferase

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Chains: C, D
Length: 135 amino acids
Theoretical weight: 14.83 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: P20023 (Residues: 19-153; Coverage: 13%)
Gene names: C3DR, CR2
Pfam: Sushi repeat (SCR repeat)
InterPro:
CATH: Complement Module, domain 1

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