MolNFT v1 · #182749 · protein
Protofilaments of microtubule doublets bound to outer-arm dynein
7N32: “Protofilaments of microtubule doublets bound to outer-arm dynein”. Electron microscopy, 3 ligands (GTP, GDP, MG). MolNFT v1 #182749 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 7N32
- Type
- protein
- Length
- 10,460 residues
- Chains
- 24
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P41351, P41352
- Ligands
- GTP, GDP, MG
Structure
electron microscopy · 5 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| w, u, s, q, o, m, k, g, e, c, a, i | — | protein | 440 | — | P41351 |
| x, v, t, r, l, h, f, b, j | — | protein | 430 | — | P41352 |
| p | — | protein | 428 | — | P41352 |
| n | — | protein | 440 | — | P41352 |
| d | — | protein | 442 | — | 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.
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
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.