Structure analysis

Crystal structure of the artificial protein AFFinger p17 (AF.p17) complexed with Fc fragment of human IgG

X-ray diffraction
2.9Å resolution
Assembly composition:
hetero tetramer (preferred)
Entry contents: 2 distinct polypeptide molecules

Assemblies

Assembly 1 (preferred)
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Multimeric state: hetero tetramer

Binding statistics and energies are not available for this assembly
Assembly 2
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Multimeric state: hetero tetramer
Accessible surface area: 25800 Å2
Buried surface area: 10900 Å2
Dissociation area: 700 Å2
Dissociation energy (ΔGdiss): 3 kcal/mol
Dissociation entropy (TΔSdiss): 11 kcal/mol
Interface energy (ΔGint): 47 kcal/mol
Symmetry number: 1
Assembly 3
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Multimeric state: hetero tetramer

Binding statistics and energies are not available for this assembly
Assembly 4
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Multimeric state: hetero tetramer
Accessible surface area: 26500 Å2
Buried surface area: 10900 Å2
Dissociation area: 1,500 Å2
Dissociation energy (ΔGdiss): 7 kcal/mol
Dissociation entropy (TΔSdiss): 21 kcal/mol
Interface energy (ΔGint): 46 kcal/mol
Symmetry number: 2

Macromolecules

Chains: A, B, C, D, I, J, M, N
Length: 212 amino acids
Theoretical weight: 23.98 KDa
Source organism: Homo sapiens
Expression system: Cricetulus griseus
UniProt:
  • Canonical: P01857 (Residues: 119-330; Coverage: 64%)
Gene name: IGHG1
Pfam: Immunoglobulin C1-set domain
InterPro:
CATH: Immunoglobulins

Search similar proteins

Chains: E, F, G, H, K, L, O, P
Length: 54 amino acids
Theoretical weight: 6.12 KDa
Source organism: synthetic construct
Expression system: Escherichia coli BL21(DE3)
CATH: N-terminal domain of TfIIb

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