Structure analysis

Structural Characterization of Minor Ampullate Spidroin Domains and their Distinct Roles in Fibroin Solubility and Fiber Formation

Solution NMR
Source organism: Trichonephila antipodiana
Assembly composition:
homo dimer (preferred)
Entry contents: 1 distinct polypeptide molecule

Assemblies

Assembly 1 (preferred)
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Multimeric state: homo dimer
Accessible surface area: 8887.23 Å2
Buried surface area: 4004.77 Å2
Dissociation area: 2,002.39 Å2
Dissociation energy (ΔGdiss): 33.15 kcal/mol
Dissociation entropy (TΔSdiss): 11.75 kcal/mol
Symmetry number: 2
PDBe Complex ID: PDB-CPX-173703

Macromolecules

Chains: A, B
Length: 107 amino acids
Theoretical weight: 10.51 KDa
Source organism: Trichonephila antipodiana
Expression system: Escherichia coli
UniProt:
  • Canonical: Q2LC34 (Residues: 250-356; Coverage: 30%)
Pfam: Major ampullate spidroin 1 and 2
InterPro:
CATH: Spidroin domain, C-terminal domain

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