Research workbench
Human cyclic gmp-AMP synthase (cgas) in complex with gamp
Analyse Human cyclic gmp-AMP synthase (cgas) in complex with gamp in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4O67
- Type
- protein
- Length
- 693 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cyclic gmp-AMP synthase
- UniProt
- Q8N884
- Ligands
- 1SY, ZN
- Pockets
- 9 · best druggability 0.80
Structure
x-ray diffraction · 2 distinct chains · 44% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cyclic gmp-AMP synthase | protein | 346 | 44% helix, 18% strand | Q8N884 |
| B | Cyclic gmp-AMP synthase | protein | 347 | 45% helix, 18% strand | Q8N884 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
9 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1055 | 0.80 | 0.81 | 71 | 1SY |
| 2 | 791 | 0.78 | 0.82 | 55 | 1SY |
| 3 | 127 | 0.70 | 0.91 | 26 | empty |
| 4 | 403 | 0.62 | 0.77 | 30 | empty |
| 5 | 165 | 0.45 | 0.76 | 22 | empty |
Interfaces
1 interface between chains.
- A–B · 423 Ų buried · 3 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 Q8N884
- Elsewhere: RCSB PDB 4O67 · PDBe 4O67 · UniProt Q8N884
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.