MolNFT v1 · #26621 · protein
Crystal structure of native canavalia gladiata lectin (cgl): a tetrameric cona-like lectin
1WUV · Concanavalin a: “Crystal structure of native canavalia gladiata lectin (cgl): a tetrameric cona-like lectin”. X-ray diffraction, 2 ligands (MN, CA), 3 pockets (best druggability 0.53). MolNFT v1 #26621 on GenesisL1: 3D structure…
- PDB
- 1WUV
- Type
- protein
- Length
- 948 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Concanavalin a
- UniProt
- P14894
- Ligands
- MN, CA
- Pockets
- 3 · best druggability 0.53
Structure
x-ray diffraction · 1 distinct chain · 5% helix, 46% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, D, G, J | Concanavalin a | protein | 237 | 5% helix, 46% strand | P14894 |
Ligands and binding sites
- MN · Manganese (II) ion · metal · 4 copies · chains A, D, G, J
- CA · Calcium ion · metal · 4 copies · chains A, D, G, J
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 273 | 0.53 | 0.75 | 42 | empty |
| 2 | 157 | 0.50 | 0.79 | 26 | empty |
| 3 | 182 | 0.44 | 0.74 | 27 | empty |
Interfaces
3 interfaces between chains.
- A–J · 1179 Ų buried · 28 hydrogen bonds · protein-protein
- D–G · 1172 Ų buried · 28 hydrogen bonds · protein-protein
- A–D · 399 Ų buried · 7 hydrogen bonds · protein-protein
Compared structures
- 1WUV · Crystal structure of native Canavalia gladiata lectin (CGL): a tetrameric ConA-like lectin · the same entry in another collection · chain J against J, TM-score 1.00
- P14894 · AlphaFold monomer V2.0 prediction for concanavalin-a (P14894) · 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 P14894
- Elsewhere: RCSB PDB 1WUV · PDBe 1WUV · UniProt P14894
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