Structure analysis

Selection of a novel highly specific TNFalpha antagonist: Insight from the crystal structure of the antagonist-TNFalpha complex

X-ray diffraction
2.1Å resolution
Source organism: Homo sapiens
Assembly composition:
hetero dimer (preferred)
Entry contents: 2 distinct polypeptide molecules

Assemblies

Assembly 1 (preferred)
Download    3D Visualisation
Multimeric state: hetero dimer
Accessible surface area: 13800 Å2
Buried surface area: 1800 Å2
Dissociation area: 850 Å2
Dissociation energy (ΔGdiss): -5 kcal/mol
Dissociation entropy (TΔSdiss): 11 kcal/mol
Interface energy (ΔGint): -6 kcal/mol
Symmetry number: 1

Macromolecules

Chain: C
Length: 134 amino acids
Theoretical weight: 15.31 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P05452 (Residues: 67-201; Coverage: 74%)
Gene names: CLEC3B, TNA
Pfam: Lectin C-type domain
InterPro:
CATH: Mannose-Binding Protein A, subunit A

Search similar proteins

Chain: T
Length: 149 amino acids
Theoretical weight: 16.5 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P01375 (Residues: 85-233; Coverage: 64%)
Gene names: TNF, TNFA, TNFSF2
Pfam: TNF(Tumour Necrosis Factor) family
InterPro:
CATH: Jelly Rolls

Search similar proteins