Structure of a carvoxamide compound (15) (N-[4-(ISOQUINOLIN-7-YL)PYRIDIN-2-YL]CYCLOPROPANECARBOXAMIDE) to GSK3b. Determined by X-ray diffraction at 2.03 Å resolution. Released 8 Apr 2015.
Explore 4PTE in 3D Show helices and sheets RCSB PDB PDBe
4PTE contains 44 α-helices and 28 β-strands across 2 chains. 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 | 38-44 | 7 | 1 |
| β-strand | 52-65 | 14 | 1 |
| β-strand | 68-75 | 8 | 1 |
| β-strand | 81-88 | 8 | 1 |
| α-helix | 96-103 | 8 | |
| β-strand | 109 | 1 | 2 |
| β-strand | 112-118 | 7 | 1 |
| β-strand | 127-133 | 7 | 1 |
| β-strand | 137-138 | 2 | 2 |
| α-helix | 139-148 | 10 | |
| α-helix | 152-154 | 3 | |
| α-helix | 155-174 | 20 | |
| β-strand | 177-178 | 2 | 3 |
| α-helix | 184-186 | 3 | |
| β-strand | 187-190 | 4 | 2 |
| β-strand | 195-198 | 4 | 2 |
| β-strand | 205-206 | 2 | 3 |
| β-strand | 219 | 1 | 4 |
| α-helix | 225-228 | 4 | |
| α-helix | 237-252 | 16 | |
| β-strand | 261 | 1 | 5 |
| α-helix | 262-273 | 12 | |
| α-helix | 276-277 | 2 | |
| α-helix | 278-284 | 7 | |
| α-helix | 297-300 | 4 | |
| α-helix | 301-304 | 4 | |
| α-helix | 311-320 | 10 | |
| α-helix | 325-327 | 3 | |
| α-helix | 329-330 | 2 | |
| α-helix | 331-335 | 5 | |
| α-helix | 338-344 | 7 | |
| α-helix | 355-357 | 3 | |
| α-helix | 364-367 | 4 | |
| α-helix | 371-373 | 3 | |
| α-helix | 374-377 | 4 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 38-44 | 7 | 6 |
| β-strand | 52-65 | 14 | 6 |
| β-strand | 68-75 | 8 | 6 |
| β-strand | 81-88 | 8 | 6 |
| α-helix | 89-90 | 2 | |
| α-helix | 96-101 | 6 | |
| β-strand | 109 | 1 | 7 |
| β-strand | 112-118 | 7 | 6 |
| β-strand | 127-133 | 7 | 6 |
| β-strand | 137-138 | 2 | 7 |
| α-helix | 139-148 | 10 | |
| α-helix | 155-173 | 19 | |
| β-strand | 177-178 | 2 | 8 |
| α-helix | 184-186 | 3 | |
| β-strand | 187-190 | 4 | 7 |
| β-strand | 195-198 | 4 | 7 |
| β-strand | 205-206 | 2 | 8 |
| β-strand | 219 | 1 | 5 |
| α-helix | 225-228 | 4 | |
| α-helix | 237-252 | 16 | |
| β-strand | 261 | 1 | 4 |
| α-helix | 262-273 | 12 | |
| α-helix | 276-277 | 2 | |
| α-helix | 278-284 | 7 | |
| α-helix | 297-300 | 4 | |
| α-helix | 301-303 | 3 | |
| α-helix | 311-320 | 10 | |
| α-helix | 325-327 | 3 | |
| α-helix | 329-330 | 2 | |
| α-helix | 331-335 | 5 | |
| α-helix | 338-340 | 3 | |
| α-helix | 341-344 | 4 | |
| α-helix | 354-357 | 4 | |
| α-helix | 364-367 | 4 | |
| α-helix | 371-373 | 3 | |
| α-helix | 374-377 | 4 | |
| α-helix | 380-383 | 4 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Glycogen synthase kinase-3 beta | A, B | protein | 441 | Homo sapiens | P49841 (AlphaFold model) |
>4PTE_1 Glycogen synthase kinase-3 beta (chains A, B) MHSSHHHHHHSSGENLYFQGHMSGRPRTTSFAESCKPVQQPSAFGSMKVSRDKDGSKVTT VVATPGQGPDRPQEVSYTDTKVIGNGSFGVVYQAKLCDSGELVAIKKVLQDKRFKNRELQ IMRKLDHCNIVRLRYFFYSSGEKKDEVYLNLVLDYVPETVYRVARHYSRAKQTLPVIYVK LYMYQLFRSLAYIHSFGICHRDIKPQNLLLDPDTAVLKLCDFGSAKQLVRGEPNVSYICS RYYRAPELIFGATDYTSSIDVWSAGCVLAELLLGQPIFPGDSGVDQLVEIIKVLGTPTRE QIREMNPNYTEFKFPQIKAHPWTKVFRPRTPPEAIALCSRLLEYTPTARLTPLEACAHSF FDELRDPNVKLPNGRDTPALFNFTTQELSSNPPLATILIPPHARIQAAASTPTNATAASD ANTGDRGQTNNAASASASNST
| ID | Name | Formula | Copies |
|---|---|---|---|
| 2WF | N-[4-(isoquinolin-7-yl)pyridin-2-yl]cyclopropanecarboxamide | C18 H15 N3 O | 2 |
Discovery of new acylaminopyridines as GSK-3 inhibitors by a structure guided in-depth exploration of chemical space around a pyrrolopyridinone core. Sivaprakasam, P., Han, X., Civiello, R.L. et al. Bioorg Med Chem Lett (2015) 25:1856-1863. DOI 10.1016/j.bmcl.2015.03.046 · PubMed
Other PDB entries of the same protein (UniProt P49841 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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