Research workbench
Joint X-RAY/NEUTRON structure of concanavalin a with ALPHA1-2 D- mannobiose
Analyse Joint X-RAY/NEUTRON structure of concanavalin a with ALPHA1-2 D- mannobiose in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5WEY
- Type
- protein
- Length
- 237 residues
- Chains
- 1
- Method
- x-ray diffraction; neutron diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Concanavalin-a
- UniProt
- P02866
- Ligands
- MAN, MN, CA
Structure
x-ray diffraction; neutron diffraction · 1 distinct chain · 5% helix, 46% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Concanavalin-a | protein | 237 | 5% helix, 46% strand | P02866 |
Ligands and binding sites
- MAN · alpha-D-mannopyranose · sugar · 2 copies · chains A
- MN · Manganese (II) ion · metal · chains A
- CA · Calcium ion · metal · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 5WEY · Joint X-ray/neutron structure of Concanavalin A with alpha1-2 D-mannobiose · the same entry in another collection · chain A against A, TM-score 1.00
- P02866 · AlphaFold monomer V2.0 prediction for concanavalin-a (P02866) · a predicted model of the same protein · chain A against A, TM-score 0.50
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 P02866
- Elsewhere: RCSB PDB 5WEY · PDBe 5WEY · UniProt P02866
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