Research workbench
Sfsting with cgamp (masked)
Analyse Sfsting with cgamp (masked) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7UNA
- Type
- protein
- Length
- 1,132 residues
- Chains
- 8
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- CD-ntase-associated protein 12
- EC
- 3.2.2.5
- UniProt
- A0A2T5Y4G4
- Ligands
- 4BW
- Pockets
- 18 · best druggability 0.83
Structure
electron microscopy · 8 distinct chains · 47% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | CD-ntase-associated protein 12 (EC 3.2.2.5) | protein | 142 | 46% helix, 22% strand | A0A2T5Y4G4 |
| B | CD-ntase-associated protein 12 (EC 3.2.2.5) | protein | 141 | 48% helix, 14% strand | A0A2T5Y4G4 |
| C | CD-ntase-associated protein 12 (EC 3.2.2.5) | protein | 143 | 45% helix, 21% strand | A0A2T5Y4G4 |
| D | CD-ntase-associated protein 12 (EC 3.2.2.5) | protein | 143 | 46% helix, 17% strand | A0A2T5Y4G4 |
| E | CD-ntase-associated protein 12 (EC 3.2.2.5) | protein | 140 | 49% helix, 20% strand | A0A2T5Y4G4 |
| F | CD-ntase-associated protein 12 (EC 3.2.2.5) | protein | 141 | 48% helix, 18% strand | A0A2T5Y4G4 |
| G | CD-ntase-associated protein 12 (EC 3.2.2.5) | protein | 141 | 48% helix, 20% strand | A0A2T5Y4G4 |
| H | CD-ntase-associated protein 12 (EC 3.2.2.5) | protein | 141 | 48% helix, 17% strand | A0A2T5Y4G4 |
Ligands and binding sites
- 4BW · 2-amino-9-[(2r,3r,3as,5r,7ar,9r,10r,10as,12r,14ar)-9-(6-amino-9H-purin-9-yl)-3,5,10,12-tetrahydroxy-5,12-dioxidooctahydro-2H,7H-difuro[3,2-D:3',2'-J][1,3,7,9, 2,8]tetraoxadiphosphacyclododecin-2-yl]-1,9-dihydro-6H-purin-6-one · ligand · 4 copies · chains A, B, C, D, E, F, G, H
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
18 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 694 | 0.83 | 0.87 | 72 | 4BW |
| 2 | 497 | 0.78 | 0.85 | 63 | empty |
| 3 | 452 | 0.76 | 0.84 | 39 | 4BW |
| 4 | 310 | 0.75 | 0.87 | 34 | 4BW |
| 5 | 440 | 0.70 | 0.81 | 37 | 4BW |
Interfaces
11 interfaces between chains.
- C–D · 669 Ų buried · 2 hydrogen bonds · protein-protein
- G–H · 641 Ų buried · 4 hydrogen bonds · protein-protein
- A–B · 635 Ų buried · 0 hydrogen bonds · protein-protein
- E–F · 572 Ų buried · 1 hydrogen bond · protein-protein
- B–D · 441 Ų buried · 4 hydrogen bonds · protein-protein
Compared structures
- 7UNA · SfSTING with cGAMP (masked) · 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 A0A2T5Y4G4
- Elsewhere: RCSB PDB 7UNA · PDBe 7UNA · UniProt A0A2T5Y4G4
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