Research workbench
The neck-linker and alpha 7 helix of drosophila melanogaster kinesin-1 fused to EB1
Analyse The neck-linker and alpha 7 helix of drosophila melanogaster kinesin-1 fused to… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5JVU
- Type
- protein
- Length
- 145 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Chimera protein of kinesin heavy chain and microtubule- associated protein RP/EB family…
- UniProt
- P17210, Q15691
- Pockets
- 1 · best druggability 0.35
Structure
x-ray diffraction · 2 distinct chains · 81% helix, 1% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Chimera protein of kinesin heavy chain and microtubule- associated protein RP/EB family member 1 | protein | 76 | 78% helix, 3% strand | P17210, Q15691 |
| B | Chimera protein of kinesin heavy chain and microtubule- associated protein RP/EB family member 1 | protein | 69 | 86% helix, 0% strand | P17210, Q15691 |
Ligands and binding sites
- EDO · 1,2-ethanediol · additive · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 61 | 0.35 | 0.77 | 14 | EDO |
Interfaces
1 interface between chains.
- A–B · 1930 Ų buried · 11 hydrogen bonds · protein-protein
Compared structures
- 5JVU · The neck-linker and alpha 7 helix of Drosophila melanogaster kinesin-1 fused to EB1 · the same entry in another collection · chain A against A, TM-score 1.00
- P17210 · AlphaFold monomer V2.0 prediction for kinesin heavy chain (P17210) · a predicted model of the same protein · chain B against A, TM-score 0.70
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 P17210
- Every structure of UniProt Q15691
- Elsewhere: RCSB PDB 5JVU · PDBe 5JVU · UniProt P17210 · UniProt Q15691
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