Research workbench
Crystal structure of the dynactin DCTN1 fragment involved in dynein interaction
Analyse Crystal structure of the dynactin DCTN1 fragment involved in dynein interaction in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4RFX
- Type
- protein
- Length
- 494 residues
- Chains
- 5
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Dynactin subunit 1
- UniProt
- P35458
- Pockets
- 4 · best druggability 0.57
Structure
x-ray diffraction · 5 distinct chains · 98% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Dynactin subunit 1 | protein | 100 | 96% helix, 0% strand | P35458 |
| B | Dynactin subunit 1 | protein | 98 | 98% helix, 0% strand | P35458 |
| C | Dynactin subunit 1 | protein | 101 | 98% helix, 0% strand | P35458 |
| D | Dynactin subunit 1 | protein | 100 | 98% helix, 0% strand | P35458 |
| E | Dynactin subunit 1 | protein | 95 | 98% helix, 0% strand | P35458 |
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 123 | 0.57 | 0.84 | 22 | empty |
| 2 | 112 | 0.40 | 0.75 | 21 | empty |
| 3 | 90 | 0.39 | 0.76 | 19 | empty |
| 4 | 117 | 0.38 | 0.74 | 16 | empty |
Interfaces
6 interfaces between chains.
- C–D · 2464 Ų buried · 11 hydrogen bonds · protein-protein
- A–B · 2404 Ų buried · 13 hydrogen bonds · protein-protein
- D–E · 663 Ų buried · 5 hydrogen bonds · protein-protein
- A–E · 454 Ų buried · 3 hydrogen bonds · protein-protein
- C–E · 443 Ų buried · 10 hydrogen bonds · protein-protein
Compared structures
- 4RFX · Crystal Structure of the Dynactin DCTN1 Fragment involved in Dynein Interaction · the same entry in another collection · chain C against C, TM-score 1.00
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 P35458
- Elsewhere: RCSB PDB 4RFX · PDBe 4RFX · UniProt P35458
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