1.5A X-ray structure of apo form of a catalytic domain of death-associated protein kinase. Determined by X-ray diffraction at 1.5 Å resolution. Released 1 Apr 2002.
Explore 1JKS in 3D Show helices and sheets RCSB PDB PDBe
1JKS contains 14 α-helices and 16 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 | 5 | 1 | 1 |
| α-helix | 9-11 | 3 | |
| β-strand | 13-21 | 9 | 1 |
| β-strand | 25-32 | 8 | 1 |
| β-strand | 38-45 | 8 | 1 |
| β-strand | 46 | 1 | 2 |
| α-helix | 47 | 1 | |
| β-strand | 56 | 1 | 2 |
| α-helix | 58-70 | 13 | |
| β-strand | 76 | 1 | 3 |
| β-strand | 79-84 | 6 | 1 |
| β-strand | 88-94 | 7 | 1 |
| β-strand | 100 | 1 | 3 |
| α-helix | 101-108 | 8 | |
| α-helix | 113-132 | 20 | |
| β-strand | 135-136 | 2 | 4 |
| α-helix | 142-144 | 3 | |
| β-strand | 145-147 | 3 | 3 |
| β-strand | 157-159 | 3 | 3 |
| β-strand | 166-167 | 2 | 4 |
| β-strand | 173 | 1 | 5 |
| α-helix | 181-183 | 3 | |
| α-helix | 186-189 | 4 | |
| β-strand | 194 | 1 | 5 |
| α-helix | 197-212 | 16 | |
| α-helix | 222-230 | 9 | |
| α-helix | 238-241 | 4 | |
| α-helix | 246-253 | 8 | |
| α-helix | 260-262 | 3 | |
| α-helix | 266-271 | 6 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Death-associated protein kinase | A | protein | 294 | Homo sapiens | P53355 (AlphaFold model) |
>1JKS_1 DEATH-ASSOCIATED PROTEIN KINASE (chains A) TVFRQENVDDYYDTGEELGSGQFAVVKKCREKSTGLQYAAKFIKKRRTKSSRRGVSREDI EREVSILKEIQHPNVITLHEVYENKTDVILILELVAGGELFDFLAEKESLTEEEATEFLK QILNGVYYLHSLQIAHFDLKPENIMLLDRNVPKPRIKIIDFGLAHKIDFGNEFKNIFGTP EFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANVSAVNYEFEDEYF SNTSALAKDFIRRLLVKDPKKRMTIQDSLQHPWIKPKDTQQALSSAWSHPQFEK
Crystal structures of the catalytic domain of human protein kinase associated with apoptosis and tumor suppression. Tereshko, V., Teplova, M., Brunzelle, J. et al. Nat Struct Biol (2001) 8:899-907. DOI 10.1038/nsb1001-899 · PubMed
Other PDB entries of the same protein (UniProt P53355 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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