MolNFT v1 · #156946 · protein
Human cgas catalytic domain bound with the inhibitor G108
6MJU · Cyclic gmp-AMP synthase: “Human cgas catalytic domain bound with the inhibitor G108”. X-ray diffraction, 2 ligands (JUM, ZN), 2 pockets (best druggability 0.78). MolNFT v1 #156946 on GenesisL1: 3D structure, binding sites and…
- PDB
- 6MJU
- Type
- protein
- Length
- 331 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
- JUM, ZN
- Pockets
- 2 · best druggability 0.78
Structure
x-ray diffraction · 1 distinct chain · 47% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cyclic gmp-AMP synthase (EC 2.7.7.86) | protein | 331 | 47% helix, 15% strand | Q8N884 |
Ligands and binding sites
- JUM · 1-[6,7-dichloro-9-(1H-pyrazol-4-yl)-1,3,4,5-tetrahydro-2H-pyrido[4,3-b]indol-2-yl]-2-hydroxyethan-1-one · ligand · chains A
- ZN · Zinc ion · metal · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 872 | 0.78 | 0.81 | 78 | JUM |
| 2 | 57 | 0.26 | 0.73 | 13 | 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 6MJU · PDBe 6MJU · UniProt Q8N884
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