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Determination of three crystal structures of canavalin by molecular replacement

Analyse Determination of three crystal structures of canavalin by molecular replacement in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1CAU
Type
protein
Length
365 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Canavalin
UniProt
P50477
Pockets
3 · best druggability 0.60

Structure

x-ray diffraction · 2 distinct chains · 12% helix, 41% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ACanavalinprotein18111% helix, 43% strandP50477
BCanavalinprotein18414% helix, 39% strandP50477

Pockets

3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11290.600.8526empty
21690.530.7926empty
3640.340.7717empty

Interfaces

1 interface between chains.

  • A–B · 1574 Ų buried · 22 hydrogen bonds · protein-protein

Compared structures

  • 1CAU · Determination of three crystal structures of canavalin by molecular replacement · the same entry in another collection · chain A against A, TM-score 1.00
  • P50477 · AlphaFold monomer V2.0 prediction for canavalin (P50477) · a predicted model of the same protein · chain A against A, TM-score 0.95

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