1dgw

X-ray diffraction
1.7Å resolution

Structure of the rhombohedral crystal of canavalin from jack bean

Released:
Source organism: Canavalia ensiformis
Primary publication:
X-ray diffraction and atomic force microscopy analysis of twinned crystals: rhombohedral canavalin.
Acta Crystallogr D Biol Crystallogr 57 829-39 (2001)
PMID: 11375502

Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
hetero nonamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-156194 (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
Canavalin Chain: A
Molecule details ›
Chain: A
Length: 178 amino acids
Theoretical weight: 20.64 KDa
Source organism: Canavalia ensiformis
UniProt:
  • Canonical: P50477 (Residues: 46-223; Coverage: 43%)
Sequence domains: Cupin
Structure domains: Jelly Rolls
Canavalin Chain: X
Molecule details ›
Chain: X
Length: 79 amino acids
Theoretical weight: 9.07 KDa
Source organism: Canavalia ensiformis
UniProt:
  • Canonical: P50477 (Residues: 246-324; Coverage: 19%)
Sequence domains: Cupin
Structure domains: Jelly Rolls
Canavalin Chain: Y
Molecule details ›
Chain: Y
Length: 93 amino acids
Theoretical weight: 10.27 KDa
Source organism: Canavalia ensiformis
UniProt:
  • Canonical: P50477 (Residues: 331-423; Coverage: 22%)
Sequence domains: Cupin
Structure domains: Arc Repressor Mutant, subunit A

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: R3
Unit cell:
a: 136.876Å b: 136.876Å c: 76.004Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.196 0.189 0.252