Research workbench
Allosteric opening of the polypeptide-binding site when an HSP70 binds ATP
Analyse Allosteric opening of the polypeptide-binding site when an HSP70 binds ATP in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4JNF
- Type
- protein
- Length
- 213 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- HSP70 chaperone dnak
- UniProt
- P0A6Y8
- Pockets
- 2 · best druggability 0.54
Structure
x-ray diffraction · 1 distinct chain · 45% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | HSP70 chaperone dnak | protein | 213 | 45% helix, 26% strand | P0A6Y8 |
Pockets
2 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 238 | 0.54 | 0.77 | 31 | empty |
| 2 | 133 | 0.50 | 0.79 | 20 | empty |
Compared structures
- 4JNF · Allosteric opening of the polypeptide-binding site when an Hsp70 binds ATP · the same entry in another collection · chain A against A, TM-score 1.00
- P0A6Y8 · AlphaFold monomer V2.0 prediction for chaperone protein dnak (P0A6Y8) · a predicted model of the same protein · chain A against A, TM-score 0.46
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 P0A6Y8
- Elsewhere: RCSB PDB 4JNF · PDBe 4JNF · UniProt P0A6Y8
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