Research workbench
Crystal structure of a lectin from canavalia brasiliensis seed (conbr) complexed with alpha-aminobutyric acid
Analyse Crystal structure of a lectin from canavalia brasiliensis seed (conbr)… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3JU9
- Type
- protein
- Length
- 237 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Concanavalin-br
- UniProt
- P55915
- Ligands
- DBB, CA, MN, CL
Structure
x-ray diffraction · 1 distinct chain · 3% helix, 45% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Concanavalin-br | protein | 237 | 3% helix, 45% strand | P55915 |
Ligands and binding sites
- DBB · D-alpha-aminobutyric acid · ligand · chains A
- CA · Calcium ion · metal · chains A
- MN · Manganese (II) ion · metal · chains A
- CL · Chloride ion · ion · 2 copies · chains A
- GOL · Glycerol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 3JU9 · Crystal structure of a lectin from Canavalia brasiliensis seed (ConBr) complexed with… · the same entry in another collection · chain A against A, TM-score 1.00
- P55915 · AlphaFold monomer V2.0 prediction for concanavalin-br (P55915) · a predicted model of the same protein · chain A against A, TM-score 0.99
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt P55915
- Elsewhere: RCSB PDB 3JU9 · PDBe 3JU9 · UniProt P55915
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