Research workbench
The structure of a yeast DYN2-NUP159 complex and the molecular basis for the dynein light chain - nuclear pore interaction
Analyse The structure of a yeast DYN2-NUP159 complex and the molecular basis for the… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4DS1
- Type
- protein
- Length
- 193 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Dynein light chain 1, cytoplasmic; Nucleoporin NUP159
- UniProt
- Q02647, P40477
Structure
x-ray diffraction · 3 distinct chains · 31% helix, 46% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C | Dynein light chain 1, cytoplasmic | protein | 86 | 38% helix, 42% strand | Q02647 |
| B | Nucleoporin NUP159 | protein | 10 | 0% helix, 60% strand | P40477 |
| D | Nucleoporin NUP159 | protein | 11 | 0% helix, 64% strand | P40477 |
Interfaces
5 interfaces between chains.
- A–C · 957 Ų buried · 29 hydrogen bonds · protein-protein
- C–D · 725 Ų buried · 20 hydrogen bonds · protein-protein
- A–B · 692 Ų buried · 21 hydrogen bonds · protein-protein
- B–C · 276 Ų buried · 4 hydrogen bonds · protein-protein
- A–D · 212 Ų buried · 3 hydrogen bonds · protein-protein
Compared structures
- 4DS1 · The Structure of a Yeast Dyn2-Nup159 Complex and the Molecular Basis for the Dynein Light… · the same entry in another collection · chain D against D, TM-score 1.00
- Q02647 · AlphaFold monomer V2.0 prediction for dynein light chain 1, cytoplasmic (Q02647) · a predicted model of the same protein · chain C against A, TM-score 0.98
- P40477 · AlphaFold monomer V2.0 prediction for nucleoporin NUP159 (P40477) · a predicted model of the same protein · chain B against A, TM-score 0.49
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 Q02647
- Every structure of UniProt P40477
- Elsewhere: RCSB PDB 4DS1 · PDBe 4DS1 · UniProt Q02647 · UniProt P40477
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