Research workbench
Middle domain of HSP90
Analyse Middle domain of HSP90 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1HK7
- Type
- protein
- Length
- 495 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Heat shock protein HSP82
- UniProt
- P02829
- Ligands
- CD, MG
- Pockets
- 7 · best druggability 0.79
Structure
x-ray diffraction · 2 distinct chains · 38% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Heat shock protein HSP82 | protein | 248 | 37% helix, 19% strand | P02829 |
| B | Heat shock protein HSP82 | protein | 247 | 38% helix, 21% strand | P02829 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
7 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 660 | 0.79 | 0.84 | 69 | empty |
| 2 | 184 | 0.51 | 0.78 | 33 | empty |
| 3 | 79 | 0.48 | 0.83 | 19 | empty |
| 4 | 131 | 0.38 | 0.73 | 27 | empty |
| 5 | 73 | 0.33 | 0.75 | 15 | empty |
Interfaces
1 interface between chains.
- A–B · 723 Ų buried · 13 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 P02829
- Elsewhere: RCSB PDB 1HK7 · PDBe 1HK7 · UniProt P02829
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