Research workbench
Tsx structure
Analyse Tsx structure in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1TLY
- Type
- protein
- Length
- 499 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Nucleoside-specific channel-forming protein tsx
- UniProt
- P0A927
- Pockets
- 3 · best druggability 0.84
Structure
x-ray diffraction · 2 distinct chains · 3% helix, 64% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Nucleoside-specific channel-forming protein tsx | protein | 251 | 3% helix, 63% strand | P0A927 |
| B | Nucleoside-specific channel-forming protein tsx | protein | 248 | 3% helix, 65% strand | P0A927 |
Pockets
3 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1167 | 0.84 | 0.85 | 97 | empty |
| 2 | 1105 | 0.83 | 0.84 | 89 | empty |
| 3 | 1020 | 0.76 | 0.77 | 66 | empty |
Interfaces
1 interface between chains.
- A–B · 331 Ų buried · 0 hydrogen bonds · protein-protein
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 P0A927
- Elsewhere: RCSB PDB 1TLY · PDBe 1TLY · UniProt P0A927
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