Research workbench
Human ATL1 mutant - R77A / F151S bound to GDP
Analyse Human ATL1 mutant - R77A / F151S bound to GDP in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6B9E
- Type
- protein
- Length
- 779 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Atlastin-1
- EC
- 3.6.5.-
- UniProt
- Q8WXF7
- Ligands
- GDP, MG, SO4
- Pockets
- 10 · best druggability 0.58
Structure
x-ray diffraction · 2 distinct chains · 50% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Atlastin-1 (EC 3.6.5.-) | protein | 392 | 49% helix, 16% strand | Q8WXF7 |
| B | Atlastin-1 (EC 3.6.5.-) | protein | 387 | 50% helix, 17% strand | Q8WXF7 |
Ligands and binding sites
- GDP · Guanosine-5'-diphosphate · ligand · 2 copies · chains A, B
- MG · Magnesium ion · metal · 2 copies · chains A, B
- SO4 · Sulfate ion · ion · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
10 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 355 | 0.58 | 0.76 | 48 | empty |
| 2 | 190 | 0.50 | 0.77 | 29 | GDP |
| 3 | 151 | 0.48 | 0.77 | 26 | empty |
| 4 | 143 | 0.46 | 0.77 | 25 | GDP |
| 5 | 105 | 0.45 | 0.79 | 20 | empty |
Interfaces
1 interface between chains.
- A–B · 509 Ų buried · 5 hydrogen bonds · protein-protein
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 Q8WXF7
- Elsewhere: RCSB PDB 6B9E · PDBe 6B9E · UniProt Q8WXF7
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