Research workbench
Tsx structure complexed with thymidine
Analyse Tsx structure complexed with thymidine in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1TLW
- 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
- Ligands
- THM
- Pockets
- 3 · best druggability 0.83
Structure
x-ray diffraction · 2 distinct chains · 3% helix, 62% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Nucleoside-specific channel-forming protein tsx | protein | 251 | 3% helix, 62% strand | P0A927 |
| B | Nucleoside-specific channel-forming protein tsx | protein | 248 | 3% helix, 62% strand | P0A927 |
Ligands and binding sites
- THM · Thymidine · ligand · 4 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
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 | 1138 | 0.83 | 0.84 | 106 | THM |
| 2 | 1097 | 0.81 | 0.82 | 101 | THM |
| 3 | 1019 | 0.75 | 0.77 | 64 | empty |
Interfaces
1 interface between chains.
- A–B · 330 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 1TLW · PDBe 1TLW · UniProt P0A927
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