Research workbench
Structure of human cgas
Analyse Structure of human cgas in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4LEV
- Type
- protein
- Length
- 738 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cyclic gmp-AMP synthase
- EC
- 2.7.7.-
- UniProt
- Q8N884
- Ligands
- ZN
- Pockets
- 9 · best druggability 0.79
Structure
x-ray diffraction · 1 distinct chain · 41% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Cyclic gmp-AMP synthase (EC 2.7.7.-) | protein | 369 | 41% helix, 17% strand | Q8N884 |
Ligands and binding sites
- ZN · Zinc ion · metal · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
9 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 941 | 0.79 | 0.81 | 83 | empty |
| 2 | 968 | 0.78 | 0.80 | 84 | empty |
| 3 | 450 | 0.64 | 0.77 | 47 | empty |
| 4 | 111 | 0.36 | 0.74 | 25 | empty |
| 5 | 52 | 0.35 | 0.79 | 15 | empty |
Interfaces
1 interface between chains.
- A–B · 759 Ų buried · 19 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 10 modified (engineered).
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 4LEV · PDBe 4LEV · UniProt Q8N884
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