Research workbench
Biochemical and structural characterization of the PAK1- LC8 interaction
Analyse Biochemical and structural characterization of the PAK1- LC8 interaction in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3DVT
- Type
- protein
- Length
- 512 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Dynein light chain 1, cytoplasmic
- UniProt
- Q24117
- Pockets
- 2 · best druggability 0.68
Structure
x-ray diffraction · 2 distinct chains · 39% helix, 42% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | Dynein light chain 1, cytoplasmic | protein | 85 | 39% helix, 42% strand | Q24117 |
| E, F | Dynein light chain 1, cytoplasmic | protein | 86 | 38% helix, 42% strand | Q24117 |
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 | 700 | 0.68 | 0.76 | 46 | empty |
| 2 | 54 | 0.59 | 0.92 | 16 | empty |
Interfaces
8 interfaces between chains.
- C–D · 1029 Ų buried · 20 hydrogen bonds · protein-protein
- A–B · 1010 Ų buried · 25 hydrogen bonds · protein-protein
- E–F · 990 Ų buried · 23 hydrogen bonds · protein-protein
- B–C · 430 Ų buried · 7 hydrogen bonds · protein-protein
- A–E · 339 Ų buried · 3 hydrogen bonds · protein-protein
Compared structures
- 3DVT · Biochemical and structural characterization of the PAK1- LC8 interaction · the same entry in another collection · chain F against F, TM-score 1.00
- Q24117 · AlphaFold monomer V2.0 prediction for dynein light chain 1, cytoplasmic (Q24117) · a predicted model of the same protein · chain B against A, TM-score 0.98
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 Q24117
- Elsewhere: RCSB PDB 3DVT · PDBe 3DVT · UniProt Q24117
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