MolNFT v1 · #85775 · protein
Crystal structure of wheat germ agglutinin isolectin 1 in complex with glycosylurethan
4AML: “Crystal structure of wheat germ agglutinin isolectin 1 in complex with glycosylurethan”. X-ray diffraction, 1 ligand (GYU), 3 pockets (best druggability 0.63). MolNFT v1 #85775 on GenesisL1: 3D structure, binding sites and pockets…
- PDB
- 4AML
- Type
- protein
- Length
- 341 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Agglutinin isolectin 1
- UniProt
- P10968
- Ligands
- GYU
- Pockets
- 3 · best druggability 0.63
Structure
x-ray diffraction · 2 distinct chains · 20% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Agglutinin isolectin 1 | protein | 171 | 18% helix, 22% strand | P10968 |
| B | Agglutinin isolectin 1 | protein | 170 | 22% helix, 20% strand | P10968 |
Ligands and binding sites
- GYU · 2-acetamido-2-deoxy-1-O-(propylcarbamoyl)-alpha-D-glucopyranose · ligand · 4 copies · chains A, B
- GOL · Glycerol · additive · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 78 | 0.63 | 0.91 | 19 | GOL |
| 2 | 81 | 0.62 | 0.90 | 18 | GOL |
| 3 | 69 | 0.58 | 0.89 | 26 | GYU |
Interfaces
1 interface between chains.
- A–B · 2385 Ų buried · 51 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 32 disulfide, 2 modified (disulfide, cyclization).
Compared structures
- 4AML · Crystal structure of wheat germ agglutinin isolectin 1 in complex with glycosylurethan · the same entry in another collection · chain A against A, TM-score 1.00
- P10968 · AlphaFold monomer V2.0 prediction for agglutinin isolectin 1 (P10968) · 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 P10968
- Elsewhere: RCSB PDB 4AML · PDBe 4AML · UniProt P10968
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