Research workbench
Human TMEM175 in an closed state
Analyse Human TMEM175 in an closed state in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7UNM
- Type
- protein
- Length
- 736 residues
- Chains
- 2
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- ENDOSOMAL/LYSOSOMAL potassium channel TMEM175
- UniProt
- Q9BSA9
- Ligands
- K
- Pockets
- 7 · best druggability 0.75
Structure
electron microscopy · 1 distinct chain · 81% helix, 2% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| B, A | ENDOSOMAL/LYSOSOMAL potassium channel TMEM175 | protein | 368 | 81% helix, 2% strand | Q9BSA9 |
Ligands and binding sites
- K · Potassium ion · metal · 5 copies · chains B, A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
7 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 813 | 0.75 | 0.79 | 74 | K |
| 2 | 355 | 0.70 | 0.83 | 45 | K |
| 3 | 392 | 0.63 | 0.77 | 40 | empty |
| 4 | 196 | 0.56 | 0.79 | 31 | empty |
| 5 | 219 | 0.55 | 0.79 | 22 | empty |
Interfaces
1 interface between chains.
- B–A · 3131 Ų buried · 21 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 Q9BSA9
- Elsewhere: RCSB PDB 7UNM · PDBe 7UNM · UniProt Q9BSA9
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