Research workbench
High curvature lateral interaction within a 13-protofilament, taxol stabilized microtubule
Analyse High curvature lateral interaction within a 13-protofilament, taxol stabilized… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6WVM
- Type
- protein
- Length
- 1,712 residues
- Chains
- 4
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P81947, E1BJB1
- Ligands
- GTP, GDP, TA1, MG
Structure
electron microscopy · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| C, A | — | protein | 430 | — | P81947 |
| D, B | — | protein | 426 | — | E1BJB1 |
Ligands and binding sites
- GTP · Guanosine-5'-triphosphate · ligand · 2 copies · chains C, D, A, B
- GDP · Guanosine-5'-diphosphate · ligand · 2 copies · chains D, B
- TA1 · Taxol · ligand · 2 copies · chains D, B
- MG · Magnesium ion · metal · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6WVM · High curvature lateral interaction within a 13-protofilament, Taxol stabilized microtubule · the same entry in another collection · chain C against C, 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 P81947
- Every structure of UniProt E1BJB1
- Elsewhere: RCSB PDB 6WVM · PDBe 6WVM · UniProt P81947 · UniProt E1BJB1
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