Research workbench
Structural basis of microtubule plus end tracking by XMAP215, clip-170 and EB1
Analyse Structural basis of microtubule plus end tracking by XMAP215, clip-170 and EB1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2QK0
- Type
- protein
- Length
- 73 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cap-gly domain-containing linker protein 1
- UniProt
- P30622
Structure
x-ray diffraction · 1 distinct chain · 4% helix, 41% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cap-gly domain-containing linker protein 1 | protein | 73 | 4% helix, 41% strand | P30622 |
Modifications
Observed in the structure: 1 modified (engineered).
Compared structures
- 2QK0 · Structural Basis of Microtubule Plus End Tracking by XMAP215, CLIP-170 and EB1 · the same entry in another collection · chain A against A, TM-score 1.00
- P30622 · AlphaFold monomer V2.0 prediction for cap-gly domain-containing linker protein 1 (P30622) · a predicted model of the same protein · chain A against A, TM-score 0.93
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 P30622
- Elsewhere: RCSB PDB 2QK0 · PDBe 2QK0 · UniProt P30622
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