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
- 2QJZ
- Type
- protein
- Length
- 240 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Microtubule-associated protein RP/EB family member 1
- UniProt
- Q15691
- Pockets
- 5 · best druggability 0.41
Structure
x-ray diffraction · 2 distinct chains · 63% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Microtubule-associated protein RP/EB family member 1 | protein | 121 | 62% helix, 0% strand | Q15691 |
| B | Microtubule-associated protein RP/EB family member 1 | protein | 119 | 63% helix, 0% strand | Q15691 |
Pockets
5 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 115 | 0.41 | 0.76 | 18 | empty |
| 2 | 92 | 0.40 | 0.77 | 15 | empty |
| 3 | 75 | 0.34 | 0.75 | 14 | empty |
| 4 | 74 | 0.33 | 0.75 | 17 | empty |
| 5 | 55 | 0.32 | 0.77 | 16 | empty |
Interfaces
1 interface between chains.
- A–B · 463 Ų buried · 8 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 8 modified (engineered).
Compared structures
- 2QJZ · 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
- Q15691 · AlphaFold monomer V2.0 prediction for microtubule-associated protein RP/EB family member… · a predicted model of the same protein · chain A against A, TM-score 0.97
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 Q15691
- Elsewhere: RCSB PDB 2QJZ · PDBe 2QJZ · UniProt Q15691
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