MolNFT v1 · #125666 · protein
Myelin-associated glycoprotein (mag) glycosylated and lysine- methylated full extracellular domain
5LFU: “Myelin-associated glycoprotein (mag) glycosylated and lysine- methylated full extracellular domain”. X-ray diffraction, 4 ligands (NAG, MAN, BMA), 1 pocket (best druggability 0.37). MolNFT v1 #125666 on GenesisL1: 3D structure…
- PDB
- 5LFU
- Type
- protein
- Length
- 487 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Myelin-associated glycoprotein
- UniProt
- P20917
- Ligands
- NAG, MAN, BMA, FUC
- Pockets
- 1 · best druggability 0.37
Structure
x-ray diffraction · 1 distinct chain · 2% helix, 48% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Myelin-associated glycoprotein | protein | 487 | 2% helix, 48% strand | P20917 |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 8 copies · chains A
- MAN · alpha-D-mannopyranose · sugar · 3 copies · chains A
- BMA · beta-D-mannopyranose · sugar · chains A
- FUC · alpha-L-fucopyranose · sugar · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 86 | 0.37 | 0.76 | 21 | empty |
Modifications
Observed in the structure: 7 disulfide, 7 glycan (disulfide, N-glycosylation, C-mannosylation).
Compared structures
- 5LFU · Myelin-associated glycoprotein (MAG) glycosylated and lysine-methylated full… · the same entry in another collection · chain A against A, TM-score 1.00
- P20917 · AlphaFold monomer V2.0 prediction for myelin-associated glycoprotein (P20917) · a predicted model of the same protein · chain A against A, TM-score 0.94
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 P20917
- Elsewhere: RCSB PDB 5LFU · PDBe 5LFU · UniProt P20917
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.