How potassium affects the activity of the molecular chaperone HSC70. II. Potassium binds specifically in the atpase active site. Determined by X-ray diffraction at 1.7 Å resolution. Released 31 Jul 1995.
Explore 1HPM in 3D Show helices and sheets RCSB PDB PDBe
1HPM contains 17 α-helices and 20 β-strands across 1 chain. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 7-10 | 4 | 1 |
| β-strand | 15-16 | 2 | 2 |
| β-strand | 17-22 | 6 | 1 |
| β-strand | 25-28 | 4 | 1 |
| α-helix | 29-30 | 2 | |
| β-strand | 38-39 | 2 | 2 |
| β-strand | 42-44 | 3 | 3 |
| β-strand | 49-51 | 3 | 3 |
| α-helix | 53-56 | 4 | |
| α-helix | 63-65 | 3 | |
| β-strand | 66-67 | 2 | 3 |
| α-helix | 70-72 | 3 | |
| α-helix | 81-87 | 7 | |
| β-strand | 93-97 | 5 | 4 |
| β-strand | 100-107 | 8 | 4 |
| β-strand | 110-114 | 5 | 4 |
| α-helix | 116-135 | 20 | |
| β-strand | 141-146 | 6 | 1 |
| α-helix | 152-164 | 13 | |
| β-strand | 168-174 | 7 | 1 |
| α-helix | 175-182 | 8 | |
| β-strand | 193-200 | 8 | 5 |
| β-strand | 205-213 | 9 | 5 |
| β-strand | 216-225 | 10 | 5 |
| α-helix | 230-249 | 20 | |
| α-helix | 257-273 | 17 | |
| β-strand | 279-288 | 10 | 6 |
| β-strand | 291-298 | 8 | 6 |
| α-helix | 299-312 | 14 | |
| α-helix | 314-324 | 11 | |
| α-helix | 328-330 | 3 | |
| β-strand | 333-337 | 5 | 5 |
| α-helix | 339-342 | 4 | |
| α-helix | 344-353 | 10 | |
| α-helix | 357-359 | 3 | |
| β-strand | 360 | 1 | 5 |
| α-helix | 368-380 | 13 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| 44K atpase fragment (N-terminal) of 7O kd heat-shock cognate protein | A | protein | 386 | Bos taurus | P19120 (AlphaFold model) |
>1HPM_1 44K ATPASE FRAGMENT (N-TERMINAL) OF 7O kD HEAT-SHOCK COGNATE PROTEIN (chains A) MSKGPAVGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVA MNPTNTVFDAKRLIGRRFDDAVVQSDMKHWPFMVVNDAGRPKVQVEYKGETKSFYPEEVS SMVLTKMKEIAEAYLGKTVTNAVVTVPAYFNDSQRQATKDAGTIAGLNVLRIINEPTAAA IAYGLDKKVGAERNVLIFDLGGGTFDVSILTIEDGIFEVKSTAGDTHLGGEDFDNRMVNH FIAEFKRKHKKDISENKRAVRRLRTACERAKRTLSSSTQASIEIDSLYEGIDFYTSITRA RFEELNADLFRGTLDPVEKALRDAKLDKSQIHDIVLVGGSTRIPKIQKLLQDFFNGKELN KSINPDEAVAYGAAVQAAILSGDKSE
| ID | Name | Formula | Copies |
|---|---|---|---|
| MG | Magnesium ion | Mg | 1 |
| PO4 | Phosphate ion | O4 P | 1 |
| ADP | Adenosine-5'-diphosphate | C10 H15 N5 O10 P2 | 1 |
Water and common crystallization additives (K, CL) are not listed.
How potassium affects the activity of the molecular chaperone Hsc70. II. Potassium binds specifically in the ATPase active site. Wilbanks, S.M., McKay, D.B. J Biol Chem (1995) 270:2251-2257. DOI 10.1074/jbc.270.5.2251 · PubMed
Other PDB entries of the same protein (UniProt P19120 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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