Research workbench
Crystal structure of the Y137S mutant of GM2-activator protein
Analyse Crystal structure of the Y137S mutant of GM2-activator protein in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2AG9
- Type
- protein
- Length
- 328 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Ganglioside GM2 activator
- UniProt
- P17900
- Ligands
- MYR
- Pockets
- 4 · best druggability 0.79
Structure
x-ray diffraction · 1 distinct chain · 7% helix, 46% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Ganglioside GM2 activator | protein | 164 | 7% helix, 46% strand | P17900 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1061 | 0.79 | 0.80 | 64 | IPA |
| 2 | 1128 | 0.76 | 0.78 | 64 | IPA |
| 3 | 186 | 0.50 | 0.77 | 24 | empty |
| 4 | 66 | 0.31 | 0.75 | 15 | empty |
Interfaces
1 interface between chains.
- A–B · 280 Ų buried · 2 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 8 disulfide (disulfide).
Compared structures
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 P17900
- Elsewhere: RCSB PDB 2AG9 · PDBe 2AG9 · UniProt P17900
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.