Research workbench
Structure of hsting in complex with novel carbocyclic pyrimidine cdn-2
Analyse Structure of hsting in complex with novel carbocyclic pyrimidine cdn-2 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7KVZ
- Type
- protein
- Length
- 181 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Stimulator of interferon genes protein
- UniProt
- A0A2R3XZB7
- Ligands
- X5D
- Pockets
- 1 · best druggability 0.41
Structure
x-ray diffraction · 1 distinct chain · 45% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Stimulator of interferon genes protein | protein | 181 | 45% helix, 25% strand | A0A2R3XZB7 |
Ligands and binding sites
- X5D · (2r,5r,7r,8r,10s,12ar,14r,15as,16r)-7-(2-amino-6-oxo-1, 6-dihydro-9H-purin-9-yl)-2,10,16-trihydroxy-14-[(pyrimidin-4-yl)oxy]decahydro-2H,10H-5,8-methano-2lambda~5~,10lambda~5~-cyclopenta[l][1,3,6,9,11,2, 10]pentaoxadiphosphacyclotetradecine-2,10-dione · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 137 | 0.41 | 0.74 | 19 | X5D |
Compared structures
- 7KVZ · Structure of hSTING in complex with novel carbocyclic pyrimidine CDN-2 · the same entry in another collection · chain A against A, TM-score 1.00
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 A0A2R3XZB7
- Elsewhere: RCSB PDB 7KVZ · PDBe 7KVZ · UniProt A0A2R3XZB7
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