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TitleBinding of benzoic acid and anions within the cupin domains of the vicilin protein canavalin from jack bean (Canavalia ensiformis): Crystal structures.
Journal, issue, pagesBiochem. Biophys. Res. Commun., Vol. 524, Page 268-271, Year 2020
Publish dateDec 8, 2019 (structure data deposition date)
AuthorsMcPherson, A.
External linksBiochem. Biophys. Res. Commun. / PubMed:31983433
MethodsX-ray diffraction
Resolution1.4 - 2.8 Å
Structure data

PDB-6v7g:
Binding of Benzoic Acid and Anions Within the Cupin Domains of the Vicillin Protein Canavalin from Jack Bean (canavalia ensiformis): Crystal Structures
Method: X-RAY DIFFRACTION / Resolution: 1.4 Å

PDB-6v7j:
The C2221 crystal form of canavalin at 173 K
Method: X-RAY DIFFRACTION / Resolution: 2 Å

PDB-6v7l:
The structure of the P212121 crystal form of canavalin at 173 K
Method: X-RAY DIFFRACTION / Resolution: 2.8 Å

Chemicals

ChemComp-ACT:
ACETATE ION

ChemComp-BEZ:
BENZOIC ACID

ChemComp-CIT:
CITRIC ACID

ChemComp-HOH:
WATER

ChemComp-GOL:
GLYCEROL

ChemComp-CA:
Unknown entry

Source
  • canavalia ensiformis (jack bean)
KeywordsPLANT PROTEIN / plant proteins / ligands / salicylic acid / enzymes / storage protein / trimer / benzoic acid / enzyme / precanavalin / proteolytic cleavage / vicillim

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