Research workbench
Tau-microtubule structural ensemble based on cryoem data
Analyse Tau-microtubule structural ensemble based on cryoem data in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7PQC
- Type
- protein
- Length
- 6,466 residues
- Chains
- 15
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Tubulin beta chain; Tubulin alpha-1B chain; Isoform tau-F of microtubule-associated…
- UniProt
- P02554, Q2XVP4, P10636
- Ligands
- GDP, GTP, MG
- Pockets
- 20 · best druggability 0.84
Structure
electron microscopy · 3 distinct chains · 36% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C, E, G, I, K, M | Tubulin beta chain | protein | 445 | 45% helix, 18% strand | P02554 |
| B, D, F, H, J, L, N | Tubulin alpha-1B chain | protein | 451 | 41% helix, 18% strand | Q2XVP4 |
| O | Isoform tau-F of microtubule-associated protein tau | protein | 194 | 6% helix, 0% strand | P10636 |
Ligands and binding sites
- GDP · Guanosine-5'-diphosphate · ligand · 7 copies · chains A, B, C, D, E, F, G, H, I, J, K, L, M
- GTP · Guanosine-5'-triphosphate · ligand · 7 copies · chains A, B, C, D, E, F, G, H, I, J, K, L, M, N
- MG · Magnesium ion · metal · 7 copies · chains B, C, D, E, F, G, H, I, J, K, L, N
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 247 | 0.84 | 0.96 | 46 | GTP, MG |
| 2 | 244 | 0.83 | 0.96 | 54 | GTP |
| 3 | 585 | 0.83 | 0.88 | 89 | GDP |
| 4 | 468 | 0.83 | 0.90 | 70 | GDP |
| 5 | 199 | 0.82 | 0.96 | 43 | GTP, MG |
Interfaces
24 interfaces between chains.
- A–B · 2262 Ų buried · 44 hydrogen bonds · protein-protein
- M–N · 2170 Ų buried · 34 hydrogen bonds · protein-protein
- I–J · 2155 Ų buried · 35 hydrogen bonds · protein-protein
- E–F · 2108 Ų buried · 33 hydrogen bonds · protein-protein
- K–L · 2096 Ų buried · 33 hydrogen bonds · protein-protein
Compared structures
- 7PQC · tau-microtubule structural ensemble based on CryoEM data · the same entry in another collection · chain F against F, 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 Q2XVP4
- Every structure of UniProt P10636
- Elsewhere: RCSB PDB 7PQC · PDBe 7PQC · UniProt P02554 · UniProt Q2XVP4 · UniProt P10636
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