Research workbench
KINESIN13-microtubule ring complex
Analyse KINESIN13-microtubule ring complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3EDL
- Type
- protein
- Length
- 1,979 residues
- Chains
- 5
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P02550, P02554, Q922S8
Structure
electron microscopy · 5 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 412 | — | P02550 |
| B | — | protein | 426 | — | P02554 |
| D | — | protein | 301 | — | Q922S8 |
| F | — | protein | 421 | — | P02550 |
| G | — | protein | 419 | — | P02554 |
Compared structures
- 3EDL · Kinesin13-Microtubule Ring complex · the same entry in another collection · chain A against A, TM-score 1.00
- P02550 · AlphaFold monomer V2.0 prediction for tubulin alpha-1A chain (P02550) · a predicted model of the same protein · chain F against A, TM-score 0.99
- Q922S8 · AlphaFold monomer V2.0 prediction for kinesin-like protein KIF2C (Q922S8) · a predicted model of the same protein · chain D against A, TM-score 0.98
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 P02550
- Every structure of UniProt P02554
- Every structure of UniProt Q922S8
- Elsewhere: RCSB PDB 3EDL · PDBe 3EDL · UniProt P02550 · UniProt P02554 · UniProt Q922S8
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