Research workbench
Complex of yeast cytoplasmic dynein mtbd-high and mt without dtt
Analyse Complex of yeast cytoplasmic dynein mtbd-high and mt without dtt in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6KIO
- Type
- protein
- Length
- 968 residues
- Chains
- 3
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Tubulin beta chain; Dynein heavy chain, cytoplasmic; Tubulin alpha-1A chain
- UniProt
- P02554, P36022
- Pockets
- 14 · best druggability 0.81
Structure
electron microscopy · 3 distinct chains · 47% helix, 13% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| b | Tubulin beta chain | protein | 426 | 45% helix, 15% strand | P02554 |
| M | Dynein heavy chain, cytoplasmic | protein | 130 | 61% helix, 0% strand | P36022 |
| a | Tubulin alpha-1A chain | protein | 412 | 46% helix, 16% strand | — |
Pockets
14 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 222 | 0.81 | 0.95 | 44 | empty |
| 2 | 591 | 0.77 | 0.83 | 76 | empty |
| 3 | 60 | 0.68 | 0.96 | 20 | empty |
| 4 | 69 | 0.61 | 0.91 | 22 | empty |
| 5 | 226 | 0.54 | 0.78 | 28 | empty |
Interfaces
3 interfaces between chains.
- b–a · 1739 Ų buried · 23 hydrogen bonds · protein-protein
- M–a · 590 Ų buried · 17 hydrogen bonds · protein-protein
- b–M · 558 Ų buried · 6 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 1 disulfide (disulfide).
Compared structures
- 6KIO · Complex of yeast cytoplasmic dynein MTBD-High and MT without DTT · the same entry in another collection · chain b against b, 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 P02554
- Every structure of UniProt P36022
- Elsewhere: RCSB PDB 6KIO · PDBe 6KIO · UniProt P02554 · UniProt P36022
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