Structure analysis

The complex structure of Human IgG Fc and its binding Repebody

X-ray diffraction
3Å resolution
Assembly composition:
hetero tetramer (preferred)
Entry contents: 2 distinct polypeptide molecules

Assemblies

Assembly 1 (preferred)
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Multimeric state: hetero tetramer
Accessible surface area: 38317.97 Å2
Buried surface area: 10469.25 Å2
Dissociation area: 2,988.69 Å2
Dissociation energy (ΔGdiss): -15.63 kcal/mol
Dissociation entropy (TΔSdiss): 39.77 kcal/mol
Symmetry number: 2
PDBe Complex ID: PDB-CPX-143696

Macromolecules

Chains: A, B
Length: 256 amino acids
Theoretical weight: 28.56 KDa
Source organism: synthetic construct
Expression system: Escherichia coli
125620406080100120140160180200220240
 
100200TPIKQIFPDDAFAETIKANLKKKSVTDAVTQNELNSIDQIIANNSDIKSVQGIQYLPNVRYLALGGNKLHDISALKELTNLTYLELKWNQLQILPNGVFDKLTNLKELVLNSNQLQSLPDGVFDKLTNLTYLNLAHNQLQSLPDGVFDKLTNLTGLELCGNQLQSLPEGVFDKLTQLKDLRLYQNQLKSVPDGVFDRLTSLQYIWLHDNPWDCTCPGIRYLSEWINKHSGVVRNSAGSVAPDSAKCSGSGKPVRSI
Chains
RSRZ Outlier Chain A (auth A)
Chain A (auth A)
RSRZ Outlier Chain B (auth B)
Chain B (auth B)
Domains
Secondary structure
Interaction interfaces
Sequence conservation

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Chains: C, D
Length: 208 amino acids
Theoretical weight: 23.67 KDa
Source organism: Homo sapiens
120820406080100120140160180200
 
50100150200PSVFLFPPKPKDTLMISRTPEVTCVVVDVSHEDPEVKFNWYVDGVEVHNAKTKPREEQYNSTYRVVSVLTVLHQDWLNGKEYKCKVSNKALPAPIEKTISKAKGQPREPQVYTLPPSRDELTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSFFLYSKLTVDKSRWQQGNVFSCSVMHEALHNHYTQKSLSLSP
UniProt
P0DOX5
Chains
Domains
Secondary structure
Ligand binding sites
Interaction interfaces
Sequence conservation

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