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Crystal Structure of human cyclic GMP-AMP synthase in complex with 5-bromo-N-[[2-fluoro-5-(1-methylpyrazol-4-yl)phenyl]methyl]-2-hydroxybenzamide
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
- 7FTT
- Type
- protein
- Length
- 691 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2.235
- Source
- Homo sapiens
- Molecule
- Cyclic GMP-AMP synthase
- EC
- 2.7.7.86
- UniProt
- Q8N884
- Ligands
- YPU, ZN
- Pockets
- 5 · best druggability 0.80
Structure
x-ray diffraction · resolution 2.235 · 2 distinct chains · 45% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cyclic GMP-AMP synthase (EC 2.7.7.86) | protein | 343 | 46% helix, 17% strand | Q8N884 |
| B | Cyclic GMP-AMP synthase (EC 2.7.7.86) | protein | 348 | 44% helix, 17% strand | Q8N884 |
Ligands and binding sites
- YPU · 5-bromo-N-{[(5P)-2-fluoro-5-(1-methyl-1H-pyrazol-4-yl)phenyl]methyl}-2-hydroxybenzamide · ligand · 2 copies · chains A, B
- 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
5 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 995 | 0.80 | 0.81 | 84 | YPU |
| 2 | 1132 | 0.78 | 0.80 | 88 | YPU |
| 3 | 210 | 0.60 | 0.81 | 24 | empty |
| 4 | 94 | 0.34 | 0.74 | 24 | empty |
| 5 | 63 | 0.33 | 0.77 | 16 | empty |
Interfaces
1 interface between chains.
- A–B · 766 Ų buried · 15 hydrogen bonds · protein-protein
Compared structures
- Q8N884 · AlphaFold monomer V2.0 prediction for cyclic gmp-AMP synthase (Q8N884) · a predicted model of the same protein · chain B against A, TM-score 0.95
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 7FTT · PDBe 7FTT · UniProt Q8N884
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