Research workbench
Model of synthetic tau (R2X4) bound to the microtubule
Analyse Model of synthetic tau (R2X4) bound to the microtubule in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6CVN
- Type
- protein
- Length
- 1,322 residues
- Chains
- 4
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P02554, Q2XVP4
- Ligands
- GDP, GTP, MG
Structure
electron microscopy · 4 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 430 | — | P02554 |
| B | — | protein | 439 | — | Q2XVP4 |
| C | — | protein | 426 | — | P02554 |
| D | — | protein | 27 | — | — |
Ligands and binding sites
- GDP · Guanosine-5'-diphosphate · ligand · 2 copies · chains A, B, 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.
Compared structures
- 6CVN · Model of synthetic tau (R2x4) bound to the microtubule · 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 P02554
- Every structure of UniProt Q2XVP4
- Elsewhere: RCSB PDB 6CVN · PDBe 6CVN · UniProt P02554 · UniProt Q2XVP4
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