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Crystal Structure of human cyclic GMP-AMP synthase in complex with (Z)-N-(4-acetylphenyl)-2-cyano-3-hydroxy-3-(5-methyl-1,2-oxazol-4-yl)prop-2-enamide
Analyse Crystal Structure of human cyclic GMP-AMP synthase in complex with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7FTR
- Type
- protein
- Length
- 360 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 1.64
- Source
- Homo sapiens
- Molecule
- Cyclic GMP-AMP synthase
- EC
- 2.7.7.86
- UniProt
- Q8N884
- Ligands
- ATP, YQH, MG, ZN, SO4
- Pockets
- 2 · best druggability 0.75
Structure
x-ray diffraction · resolution 1.64 · 1 distinct chain · 43% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cyclic GMP-AMP synthase (EC 2.7.7.86) | protein | 360 | 43% helix, 19% strand | Q8N884 |
Ligands and binding sites
- ATP · Adenosine-5'-triphosphate · ligand · chains A
- YQH · (2Z)-N-(4-acetylphenyl)-2-cyano-3-hydroxy-3-(5-methyl-1,2-oxazol-4-yl)prop-2-enamide · ligand · chains A
- MG · Magnesium ion · metal · 2 copies · chains A
- ZN · Zinc ion · metal · chains A
- SO4 · Sulfate ion · ion · 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 | 881 | 0.75 | 0.78 | 65 | MG, ATP, YQH |
| 2 | 157 | 0.43 | 0.75 | 23 | empty |
Compared structures
- Q8N884 · AlphaFold monomer V2.0 prediction for cyclic gmp-AMP synthase (Q8N884) · a predicted model of the same protein · chain A against A, TM-score 0.99
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 7FTR · PDBe 7FTR · UniProt Q8N884
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