Research workbench
Cryo-EM structure of human TorsinA filament
Analyse Cryo-EM structure of human TorsinA filament in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6OIF
- Type
- protein
- Length
- 7,050 residues
- Chains
- 25
- Method
- electron microscopy
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 4.4
- Source
- Homo sapiens
- Molecule
- Torsin-1A
- EC
- 3.6.4.-
- UniProt
- O14656
- Ligands
- ATP
- Pockets
- 20 · best druggability 0.84
Structure
electron microscopy · resolution 4.4 · 1 distinct chain · 47% helix, 7% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P, Q, R, S, T, U, V, W, X, Y | Torsin-1A (EC 3.6.4.-) | protein | 282 | 47% helix, 7% strand | O14656 |
Ligands and binding sites
- ATP · Adenosine-5'-triphosphate · ligand · 25 copies · chains A, C, B, E, D, G, F, I, H, K, J, M, L, O, N, Q, P, S, R, U, T, W, V, Y, X
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1000 | 0.84 | 0.85 | 124 | ATP |
| 2 | 1035 | 0.82 | 0.83 | 96 | empty |
| 3 | 823 | 0.82 | 0.84 | 72 | empty |
| 4 | 782 | 0.82 | 0.85 | 72 | empty |
| 5 | 817 | 0.82 | 0.84 | 73 | empty |
Interfaces
57 interfaces between chains.
- P–R · 1406 Ų buried · 14 hydrogen bonds · protein-protein
- N–P · 1404 Ų buried · 14 hydrogen bonds · protein-protein
- T–V · 1404 Ų buried · 14 hydrogen bonds · protein-protein
- J–L · 1404 Ų buried · 14 hydrogen bonds · protein-protein
- O–Q · 1403 Ų buried · 14 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 25 disulfide, 24 covalent (disulfide, covalent ligand).
Compared structures
- O14656 · AlphaFold monomer V2.0 prediction for torsin-1A (O14656) · a predicted model of the same protein · chain A against A, TM-score 0.93
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 O14656
- Elsewhere: RCSB PDB 6OIF · PDBe 6OIF · UniProt O14656
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