MolNFT v1 · #148068 · protein
Cryo-EM structure of GDP-microtubule co-polymerised with doublecortin and supplemented with taxol
6EW0: “Cryo-EM structure of GDP-microtubule co-polymerised with doublecortin and supplemented with taxol”. Electron microscopy, 4 ligands (GTP, GDP, TA1). MolNFT v1 #148068 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 6EW0
- Type
- protein
- Length
- 5,166 residues
- Chains
- 12
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q2XVP4, P02554
- Ligands
- GTP, GDP, TA1, MG
Structure
electron microscopy · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| E, J, C, L, A, K | — | protein | 432 | — | Q2XVP4 |
| F, G, D, I, B, H | — | protein | 429 | — | P02554 |
Ligands and binding sites
- GTP · Guanosine-5'-triphosphate · ligand · 6 copies · chains E, G, F, J, C, I, L, A, K, B
- GDP · Guanosine-5'-diphosphate · ligand · 6 copies · chains E, F, G, C, D, I, A, B, H
- TA1 · Taxol · ligand · 6 copies · chains F, G, D, I, B, H
- MG · Magnesium ion · metal · 6 copies · chains E, J, C, L, A, K
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6EW0 · Cryo-EM structure of GDP-microtubule co-polymerised with doublecortin and supplemented… · the same entry in another collection · chain E against E, 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 6EW0 · PDBe 6EW0 · UniProt Q2XVP4 · UniProt P02554
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