Research workbench
AlphaFold monomer V2.0 prediction for vascular endothelial growth factor receptor 3 (Q5MD89)
Analyse AlphaFold monomer V2.0 prediction for vascular endothelial growth factor… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q5MD89
- Type
- protein
- Length
- 1,357 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xbDA05C32aD6eE153C8C5A78dfa48d7Ba25694fea
- Molecule
- Vascular endothelial growth factor receptor 3
- UniProt
- Q5MD89
- Pockets
- 10 · best druggability 0.70
Structure
1 distinct chain · 14% helix, 34% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Vascular endothelial growth factor receptor 3 | protein | 1357 | 14% helix, 34% strand | Q5MD89 |
Pockets
10 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 476 | 0.70 | 0.81 | 65 | empty |
| 2 | 355 | 0.68 | 0.81 | 38 | empty |
| 3 | 358 | 0.59 | 0.77 | 34 | empty |
| 4 | 227 | 0.58 | 0.79 | 33 | empty |
| 5 | 127 | 0.39 | 0.74 | 17 | empty |
Modifications
Observed in the structure: 10 disulfide (disulfide).
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 Q5MD89
- Elsewhere: UniProt Q5MD89 · AlphaFold DB Q5MD89
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.