Research workbench
How potassium affects the activity of the molecular chaperone HSC70. II. potassium binds specifically in the ATPase active site
Analyse How potassium affects the activity of the molecular chaperone HSC70. II.… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1HPM
- Type
- protein
- Length
- 378 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- 44K ATPase fragment (N-terminal) of 7O kd heat- shock cognate protein
- EC
- 3.6.1.3
- UniProt
- P19120
- Ligands
- ADP, K, MG, CL, PO4
- Pockets
- 1 · best druggability 0.76
Structure
x-ray diffraction · 1 distinct chain · 40% helix, 29% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | 44K ATPase fragment (N-terminal) of 7O kd heat- shock cognate protein (EC 3.6.1.3) | protein | 378 | 40% helix, 29% strand | P19120 |
Ligands and binding sites
- ADP · Adenosine-5'-diphosphate · ligand · chains A
- K · Potassium ion · metal · 2 copies · chains A
- MG · Magnesium ion · metal · chains A
- CL · Chloride ion · ion · 2 copies · chains A
- PO4 · Phosphate ion · ion · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 764 | 0.76 | 0.81 | 74 | MG, PO4, K, ADP |
Compared structures
- 1HPM · How potassium affects the activity of the molecular chaperone HSC70. II. potassium binds… · the same entry in another collection · chain A against A, TM-score 1.00
- P19120 · AlphaFold monomer V2.0 prediction for heat shock cognate 71 kda protein (P19120) · a predicted model of the same protein · chain A against A, TM-score 0.89
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 P19120
- Elsewhere: RCSB PDB 1HPM · PDBe 1HPM · UniProt P19120
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