Research workbench
Crystal structure of SAR1-GDP complex
Analyse Crystal structure of SAR1-GDP complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1F6B
- Type
- protein
- Length
- 356 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- SAR1
- UniProt
- Q9QVY3
- Ligands
- GDP, MG, SO4
- Pockets
- 4 · best druggability 0.49
Structure
x-ray diffraction · 2 distinct chains · 33% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | SAR1 | protein | 176 | 32% helix, 23% strand | Q9QVY3 |
| B | SAR1 | protein | 180 | 34% helix, 21% strand | Q9QVY3 |
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 · 5 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 147 | 0.49 | 0.78 | 32 | MG |
| 2 | 175 | 0.48 | 0.76 | 20 | empty |
| 3 | 93 | 0.40 | 0.77 | 19 | empty |
| 4 | 68 | 0.33 | 0.76 | 18 | MG, GDP |
Interfaces
1 interface between chains.
- A–B · 784 Ų buried · 14 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 Q9QVY3
- Elsewhere: RCSB PDB 1F6B · PDBe 1F6B · UniProt Q9QVY3
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.