Research workbench
Crystal structure of HSP104 R328M/R757M mutant from calcarisporiella thermophila
Analyse Crystal structure of HSP104 R328M/R757M mutant from calcarisporiella thermophila in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6AZY
- Type
- protein
- Length
- 810 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Heat shock protein HSP104
- Ligands
- ADP
- Pockets
- 9 · best druggability 0.72
Structure
x-ray diffraction · 1 distinct chain · 60% helix, 11% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Heat shock protein HSP104 | protein | 810 | 60% helix, 11% strand | — |
Ligands and binding sites
- ADP · Adenosine-5'-diphosphate · ligand · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
9 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 825 | 0.72 | 0.77 | 76 | empty |
| 2 | 218 | 0.56 | 0.78 | 24 | empty |
| 3 | 131 | 0.53 | 0.81 | 21 | empty |
| 4 | 229 | 0.53 | 0.77 | 29 | ADP |
| 5 | 189 | 0.52 | 0.78 | 29 | ADP |
Compared structures
- 6AZY · Crystal structure of Hsp104 R328M/R757M mutant from Calcarisporiella thermophila · the same entry in another collection · chain A against A, TM-score 1.00
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Elsewhere: RCSB PDB 6AZY · PDBe 6AZY
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