Structure analysis

2.2 ANGSTROMS RESOLUTION STRUCTURE ANALYSIS OF TWO REFINED N-ACETYLNEURAMINYLLACTOSE-WHEAT GERM AGGLUTININ ISOLECTIN COMPLEXES

X-ray diffraction
2Å resolution
Source organism: Triticum aestivum
Assemblies composition:
homo dimer
monomeric (preferred)
Entry contents: 1 distinct polypeptide molecule

Assemblies

Assembly 1
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Multimeric state: homo dimer
Accessible surface area: 14490.06 Å2
Buried surface area: 4571.0 Å2
Dissociation area: 2,285.5 Å2
Dissociation energy (ΔGdiss): 29.45 kcal/mol
Dissociation entropy (TΔSdiss): 12.86 kcal/mol
Symmetry number: 2
PDBe Complex ID: PDB-CPX-145544
Assembly 2 (preferred)
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Multimeric state: monomeric
Accessible surface area: 9755.66 Å2
Buried surface area: 0.0 Å2
Dissociation area: 0 Å2
Dissociation energy (ΔGdiss): 0 kcal/mol
Dissociation entropy (TΔSdiss): 0 kcal/mol
Symmetry number: 1
PDBe Complex ID: PDB-CPX-145543
Assembly 3
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Multimeric state: homo dimer
Accessible surface area: 14918.14 Å2
Buried surface area: 4599.56 Å2
Dissociation area: 2,299.78 Å2
Dissociation energy (ΔGdiss): 30.35 kcal/mol
Dissociation entropy (TΔSdiss): 12.89 kcal/mol
Symmetry number: 2
PDBe Complex ID: PDB-CPX-145544

Macromolecules

Chains: A, B
Length: 171 amino acids
Theoretical weight: 17.12 KDa
Source organism: Triticum aestivum
Expression system: Not provided
UniProt:
  • Canonical: P10968 (Residues: 27-197; Coverage: 92%)
Pfam: Chitin recognition protein
InterPro:
CATH: Endochitinase-like
SCOP: Hevein-like agglutinin (lectin) domain

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