Research workbench
Model of synthetic tau (four tandem repeats of first repeat sequence) bound to the microtubule
Analyse Model of synthetic tau (four tandem repeats of first repeat sequence) bound to… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6CVJ
- Type
- protein
- Length
- 1,308 residues
- Chains
- 4
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Tubulin alpha-1B chain; Tubulin beta chain; Microtubule-associated protein tau
- UniProt
- Q2XVP4, P02554
- Ligands
- GDP, GTP, MG
- Pockets
- 20 · best druggability 0.83
Structure
electron microscopy · 4 distinct chains · 46% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Tubulin alpha-1B chain | protein | 439 | 44% helix, 18% strand | Q2XVP4 |
| B | Tubulin beta chain | protein | 431 | 46% helix, 19% strand | P02554 |
| C | Tubulin beta chain | protein | 426 | 49% helix, 19% strand | P02554 |
| D | Microtubule-associated protein tau | protein | 12 | 0% helix, 0% strand | — |
Ligands and binding sites
- GDP · Guanosine-5'-diphosphate · ligand · 2 copies · chains B, A, C
- GTP · Guanosine-5'-triphosphate · ligand · chains A, B
- MG · Magnesium ion · metal · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 8 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 232 | 0.83 | 0.96 | 45 | GTP, MG |
| 2 | 379 | 0.79 | 0.88 | 70 | GDP |
| 3 | 57 | 0.63 | 0.93 | 22 | empty |
| 4 | 272 | 0.56 | 0.76 | 29 | empty |
| 5 | 194 | 0.55 | 0.79 | 37 | GDP |
Interfaces
4 interfaces between chains.
- A–B · 2043 Ų buried · 29 hydrogen bonds · protein-protein
- A–C · 1900 Ų buried · 25 hydrogen bonds · protein-protein
- A–D · 456 Ų buried · 6 hydrogen bonds · protein-protein
- C–D · 293 Ų buried · 4 hydrogen bonds · protein-protein
Compared structures
- 6CVJ · Model of synthetic tau (four tandem repeats of first repeat sequence) bound to the… · 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 Q2XVP4
- Every structure of UniProt P02554
- Elsewhere: RCSB PDB 6CVJ · PDBe 6CVJ · UniProt Q2XVP4 · UniProt P02554
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