Structure analysis

Crystal Structure of curculin1 homodimer

X-ray diffraction
1.5Å resolution
Source organism: Molineria latifolia
Assembly composition:
homo dimer (preferred)
Entry contents: 1 distinct polypeptide molecule

Assemblies

Assembly 1
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Multimeric state: homo dimer
Accessible surface area: 10958.06 Å2
Buried surface area: 2542.25 Å2
Dissociation area: 1,271.13 Å2
Dissociation energy (ΔGdiss): 19.4 kcal/mol
Dissociation entropy (TΔSdiss): 11.62 kcal/mol
Symmetry number: 2
PDBe Complex ID: PDB-CPX-148686
Assembly 2 (preferred)
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Multimeric state: homo dimer
Accessible surface area: 11030.45 Å2
Buried surface area: 3075.99 Å2
Dissociation area: 1,330.35 Å2
Dissociation energy (ΔGdiss): 23.38 kcal/mol
Dissociation entropy (TΔSdiss): 11.67 kcal/mol
Symmetry number: 2
PDBe Complex ID: PDB-CPX-148686

Macromolecules

Chains: A, B, C, D
Length: 115 amino acids
Theoretical weight: 12.72 KDa
Source organism: Molineria latifolia
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P19667 (Residues: 23-136; Coverage: 84%)
Gene names: CUR09, CUR37
InterPro:
CATH: Bulb-type lectin domain
PDBe-KB: UniProt Coverage View: P19667  
1115102030405060708090100110
 
50100
UniProt
P19667
Chains
Domains
Secondary structure
Flexibility predictions
Early folding residue predictions
Ligand binding sites
Interaction interfaces

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