Research workbench
Cryo-EM structure of human TMEM120A in the coash-bound state
Analyse Cryo-EM structure of human TMEM120A in the coash-bound state in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7F3T
- Type
- protein
- Length
- 660 residues
- Chains
- 2
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Transmembrane protein 120A
- UniProt
- Q9BXJ8
- Ligands
- COA
- Pockets
- 10 · best druggability 0.78
Structure
electron microscopy · 1 distinct chain · 80% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Transmembrane protein 120A | protein | 330 | 80% helix, 0% strand | Q9BXJ8 |
Ligands and binding sites
- COA · Coenzyme A · ligand · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
10 pockets found on a 1 Å grid, 8 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 868 | 0.78 | 0.81 | 63 | COA |
| 2 | 893 | 0.78 | 0.80 | 62 | COA |
| 3 | 642 | 0.70 | 0.78 | 58 | empty |
| 4 | 61 | 0.69 | 0.96 | 21 | empty |
| 5 | 59 | 0.69 | 0.96 | 20 | empty |
Interfaces
1 interface between chains.
- A–B · 3102 Ų buried · 16 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 Q9BXJ8
- Elsewhere: RCSB PDB 7F3T · PDBe 7F3T · UniProt Q9BXJ8
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