Research workbench
Yeast HSP104 fragment 1-360
Analyse Yeast HSP104 fragment 1-360 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5WBW
- Type
- protein
- Length
- 1,034 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Heat shock protein 104
- UniProt
- P31539
- Pockets
- 13 · best druggability 0.77
Structure
x-ray diffraction · 3 distinct chains · 49% helix, 10% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Heat shock protein 104 | protein | 338 | 52% helix, 10% strand | P31539 |
| B | Heat shock protein 104 | protein | 351 | 49% helix, 9% strand | P31539 |
| D | Heat shock protein 104 | protein | 345 | 45% helix, 10% strand | P31539 |
Pockets
13 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1141 | 0.77 | 0.80 | 107 | empty |
| 2 | 351 | 0.62 | 0.78 | 40 | empty |
| 3 | 387 | 0.60 | 0.76 | 31 | empty |
| 4 | 291 | 0.57 | 0.77 | 28 | empty |
| 5 | 263 | 0.55 | 0.77 | 37 | empty |
Interfaces
3 interfaces between chains.
- A–D · 702 Ų buried · 5 hydrogen bonds · protein-protein
- A–B · 481 Ų buried · 7 hydrogen bonds · protein-protein
- B–D · 117 Ų buried · 2 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 P31539
- Elsewhere: RCSB PDB 5WBW · PDBe 5WBW · UniProt P31539
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.