Research workbench
High affinity dynein microtubule binding domain - tubulin complex
Analyse High affinity dynein microtubule binding domain - tubulin complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3J1T
- Type
- protein
- Length
- 1,030 residues
- Chains
- 3
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cytoplasmic dynein 1 heavy chain 1, seryl T-RNA synthetase chimera; Tubulin alpha-1B…
- UniProt
- Q9JHU4
- Pockets
- 11 · best druggability 0.87
Structure
electron microscopy · 3 distinct chains · 49% helix, 10% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cytoplasmic dynein 1 heavy chain 1, seryl T-RNA synthetase chimera | protein | 164 | 78% helix, 1% strand | Q9JHU4 |
| B | Tubulin alpha-1B chain | protein | 439 | 43% helix, 12% strand | — |
| C | Tubulin beta-2B chain | protein | 427 | 45% helix, 12% strand | — |
Pockets
11 pockets found on a 1 Å grid, 9 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 694 | 0.87 | 0.91 | 117 | empty |
| 2 | 668 | 0.87 | 0.91 | 91 | empty |
| 3 | 962 | 0.85 | 0.86 | 103 | empty |
| 4 | 367 | 0.84 | 0.92 | 46 | empty |
| 5 | 515 | 0.84 | 0.90 | 92 | empty |
Interfaces
3 interfaces between chains.
- B–C · 1320 Ų buried · 15 hydrogen bonds · protein-protein
- A–C · 531 Ų buried · 12 hydrogen bonds · protein-protein
- A–B · 424 Ų buried · 11 hydrogen bonds · protein-protein
Compared structures
- 3J1T · High affinity dynein microtubule binding domain - tubulin complex · the same entry in another collection · chain A against A, 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 Q9JHU4
- Elsewhere: RCSB PDB 3J1T · PDBe 3J1T · UniProt Q9JHU4
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