Research workbench
Yeast TIM44 C-terminal domain complexed with cymal-3
Analyse Yeast TIM44 C-terminal domain complexed with cymal-3 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3QK9
- Type
- protein
- Length
- 349 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Mitochondrial import inner membrane translocase subunit TIM44
- UniProt
- Q01852
- Ligands
- CL
- Pockets
- 2 · best druggability 0.73
Structure
x-ray diffraction · 2 distinct chains · 38% helix, 33% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Mitochondrial import inner membrane translocase subunit TIM44 | protein | 174 | 38% helix, 30% strand | Q01852 |
| B | Mitochondrial import inner membrane translocase subunit TIM44 | protein | 175 | 38% helix, 36% strand | Q01852 |
Ligands and binding sites
- CL · Chloride ion · ion · 2 copies · chains B, A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 595 | 0.73 | 0.80 | 67 | empty |
| 2 | 458 | 0.70 | 0.80 | 54 | empty |
Interfaces
1 interface between chains.
- A–B · 682 Ų buried · 3 hydrogen bonds · protein-protein
Compared structures
- 3QK9 · Yeast Tim44 C-terminal domain complexed with Cymal-3 · the same entry in another collection · chain A against A, TM-score 1.00
- Q01852 · AlphaFold monomer V2.0 prediction for mitochondrial import inner membrane translocase… · a predicted model of the same protein · chain A against A, TM-score 0.95
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 Q01852
- Elsewhere: RCSB PDB 3QK9 · PDBe 3QK9 · UniProt Q01852
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.