Research workbench
Crystal structure of the tpr domain of KLC1 in complex with the C- terminal peptide of torsina
Analyse Crystal structure of the tpr domain of KLC1 in complex with the C- terminal… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6FV0
- Type
- protein
- Length
- 384 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Kinesin light chain 1,TORSIN-1A; Nanobody
- EC
- 3.6.4.-
- UniProt
- Q5UE59, Q9ER39
- Pockets
- 3 · best druggability 0.52
Structure
x-ray diffraction · 2 distinct chains · 55% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Kinesin light chain 1,TORSIN-1A (EC 3.6.4.-) | protein | 270 | 76% helix, 0% strand | Q5UE59, Q9ER39 |
| F | Nanobody | protein | 114 | 8% helix, 47% strand | — |
Ligands and binding sites
- PEG · Di(hydroxyethyl)ether · additive · chains A, F
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 169 | 0.52 | 0.78 | 30 | empty |
| 2 | 104 | 0.41 | 0.77 | 20 | empty |
| 3 | 55 | 0.31 | 0.76 | 11 | empty |
Interfaces
1 interface between chains.
- A–F · 869 Ų buried · 20 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 1 disulfide (disulfide).
Compared structures
- 6FV0 · Crystal structure of the TPR domain of KLC1 in complex with the C-terminal peptide of… · the same entry in another collection · chain F against F, TM-score 1.00
- Q9ER39 · AlphaFold monomer V2.0 prediction for torsin-1A (Q9ER39) · a predicted model of the same protein · chain A against A, TM-score 0.30
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 Q5UE59
- Every structure of UniProt Q9ER39
- Elsewhere: RCSB PDB 6FV0 · PDBe 6FV0 · UniProt Q5UE59 · UniProt Q9ER39
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