MolNFT v1 · #101920 · protein
Structure of human cyclic gmp-AMP synthase (cgas)
4O68: “Structure of human cyclic gmp-AMP synthase (cgas)”. X-ray diffraction, 1 ligand (ZN), 5 pockets (best druggability 0.77). MolNFT v1 #101920 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 4O68
- Type
- protein
- Length
- 353 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cyclic gmp-AMP synthase
- EC
- 2.7.7.86
- UniProt
- Q8N884
- Ligands
- ZN
- Pockets
- 5 · best druggability 0.77
Structure
x-ray diffraction · 1 distinct chain · 41% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cyclic gmp-AMP synthase (EC 2.7.7.86) | protein | 353 | 41% helix, 17% strand | Q8N884 |
Ligands and binding sites
- ZN · Zinc ion · metal · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1177 | 0.77 | 0.79 | 77 | empty |
| 2 | 69 | 0.44 | 0.82 | 22 | empty |
| 3 | 62 | 0.33 | 0.76 | 17 | empty |
| 4 | 51 | 0.32 | 0.77 | 13 | empty |
| 5 | 57 | 0.30 | 0.75 | 18 | empty |
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 4O68 · PDBe 4O68 · UniProt Q8N884
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