Research workbench
Crystal structure of hikeshi, a new nuclear transport receptor of HSP70
Analyse Crystal structure of hikeshi, a new nuclear transport receptor of HSP70 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3WVZ
- Type
- protein
- Length
- 370 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protein hikeshi
- UniProt
- Q53FT3
- Pockets
- 3 · best druggability 0.43
Structure
x-ray diffraction · 2 distinct chains · 24% helix, 32% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protein hikeshi | protein | 192 | 22% helix, 30% strand | Q53FT3 |
| B | Protein hikeshi | protein | 178 | 26% helix, 33% strand | Q53FT3 |
Pockets
3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 190 | 0.43 | 0.73 | 25 | empty |
| 2 | 65 | 0.35 | 0.77 | 16 | empty |
| 3 | 56 | 0.35 | 0.78 | 16 | empty |
Interfaces
1 interface between chains.
- A–B · 2656 Ų buried · 28 hydrogen bonds · protein-protein
Compared structures
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 Q53FT3
- Elsewhere: RCSB PDB 3WVZ · PDBe 3WVZ · UniProt Q53FT3
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