Research workbench
Protofilaments of microtubule doublets bound to outer-arm dynein
Analyse Protofilaments of microtubule doublets bound to outer-arm dynein in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7N32
- Type
- protein
- Length
- 10,460 residues
- Chains
- 24
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Tubulin alpha chain; Tubulin beta chain
- UniProt
- P41351, P41352
- Ligands
- GTP, GDP, MG
- Pockets
- 20 · best druggability 0.82
Structure
electron microscopy · 5 distinct chains · 44% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| w, u, s, q, o, m, k, g, e, c, a, i | Tubulin alpha chain | protein | 440 | 44% helix, 15% strand | P41351 |
| x, v, t, r, l, h, f, b, j | Tubulin beta chain | protein | 430 | 45% helix, 17% strand | P41352 |
| p | Tubulin beta chain | protein | 428 | 41% helix, 16% strand | P41352 |
| n | Tubulin beta chain | protein | 440 | 45% helix, 16% strand | P41352 |
| d | Tubulin beta chain | protein | 442 | 44% helix, 16% strand | P41352 |
Ligands and binding sites
- GTP · Guanosine-5'-triphosphate · ligand · 12 copies · chains w, x, u, v, s, t, q, r, o, p, m, n, k, l, g, h, e, f, c, d, a, b, i, j
- GDP · Guanosine-5'-diphosphate · ligand · 11 copies · chains x, w, v, u, t, r, q, p, o, n, l, h, i, f, c, b, k, j
- MG · Magnesium ion · metal · 12 copies · chains w, x, u, v, s, t, q, r, o, p, m, n, k, l, g, h, e, f, c, d, a, b, i, j
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 | 191 | 0.82 | 0.97 | 45 | GTP, MG |
| 2 | 185 | 0.82 | 0.97 | 42 | GTP, MG |
| 3 | 195 | 0.82 | 0.97 | 44 | GTP, MG |
| 4 | 197 | 0.82 | 0.97 | 45 | GTP, MG |
| 5 | 195 | 0.82 | 0.97 | 42 | GTP, MG |
Interfaces
38 interfaces between chains.
- o–p · 2144 Ų buried · 32 hydrogen bonds · protein-protein
- g–h · 2141 Ų buried · 28 hydrogen bonds · protein-protein
- i–j · 2133 Ų buried · 26 hydrogen bonds · protein-protein
- s–t · 2133 Ų buried · 28 hydrogen bonds · protein-protein
- w–x · 2119 Ų buried · 31 hydrogen bonds · protein-protein
Compared structures
- 7N32 · protofilaments of microtubule doublets bound to outer-arm dynein · the same entry in another collection · chain p against p, 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 P41351
- Every structure of UniProt P41352
- Elsewhere: RCSB PDB 7N32 · PDBe 7N32 · UniProt P41351 · UniProt P41352
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