Crystal structure of GSK3beta complexed with Morin. Determined by X-ray diffraction at 2.14 Å resolution. Released 19 Sept 2018.
Explore 6AE3 in 3D Show helices and sheets RCSB PDB PDBe
6AE3 contains 95 α-helices and 50 β-strands across 4 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 | 37-44 | 8 | 1 |
| β-strand | 52-64 | 13 | 1 |
| β-strand | 68-75 | 8 | 1 |
| β-strand | 81-88 | 8 | 1 |
| α-helix | 96-102 | 7 | |
| β-strand | 109 | 1 | 2 |
| β-strand | 112-119 | 8 | 1 |
| β-strand | 126-133 | 8 | 1 |
| β-strand | 137-138 | 2 | 2 |
| α-helix | 139-148 | 10 | |
| α-helix | 152-154 | 3 | |
| α-helix | 155-173 | 19 | |
| β-strand | 177-178 | 2 | 3 |
| α-helix | 184-186 | 3 | |
| β-strand | 187-189 | 3 | 2 |
| β-strand | 196-198 | 3 | 2 |
| α-helix | 201-203 | 3 | |
| β-strand | 205-206 | 2 | 3 |
| α-helix | 220-222 | 3 | |
| α-helix | 225-228 | 4 | |
| α-helix | 237-252 | 16 | |
| α-helix | 264-273 | 10 | |
| α-helix | 275-277 | 3 | |
| 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 | 354-358 | 5 | |
| α-helix | 364-367 | 4 | |
| α-helix | 371-373 | 3 | |
| α-helix | 374-377 | 4 | |
| α-helix | 380-382 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 38-44 | 7 | 4 |
| β-strand | 52-64 | 13 | 4 |
| β-strand | 68-75 | 8 | 4 |
| β-strand | 81-88 | 8 | 4 |
| α-helix | 96-102 | 7 | |
| β-strand | 109 | 1 | 5 |
| β-strand | 112-118 | 7 | 4 |
| β-strand | 127-133 | 7 | 4 |
| β-strand | 137-138 | 2 | 5 |
| α-helix | 139-148 | 10 | |
| α-helix | 155-173 | 19 | |
| β-strand | 177-178 | 2 | 6 |
| α-helix | 184-186 | 3 | |
| β-strand | 187-190 | 4 | 5 |
| β-strand | 195-198 | 4 | 5 |
| α-helix | 201-203 | 3 | |
| β-strand | 205-206 | 2 | 6 |
| α-helix | 220-222 | 3 | |
| α-helix | 225-228 | 4 | |
| α-helix | 237-252 | 16 | |
| α-helix | 264-273 | 10 | |
| α-helix | 275-277 | 3 | |
| α-helix | 278-284 | 7 | |
| α-helix | 297-300 | 4 | |
| α-helix | 301-304 | 4 | |
| α-helix | 311-318 | 8 | |
| α-helix | 325-327 | 3 | |
| α-helix | 329-330 | 2 | |
| α-helix | 331-335 | 5 | |
| α-helix | 338-344 | 7 | |
| α-helix | 354-358 | 5 | |
| α-helix | 364-367 | 4 | |
| α-helix | 371-373 | 3 | |
| α-helix | 374-377 | 4 | |
| α-helix | 380-382 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 38-44 | 7 | 7 |
| β-strand | 52-64 | 13 | 7 |
| β-strand | 68-75 | 8 | 7 |
| β-strand | 81-88 | 8 | 7 |
| α-helix | 89-90 | 2 | |
| α-helix | 96-103 | 8 | |
| β-strand | 109 | 1 | 8 |
| β-strand | 112-117 | 6 | 7 |
| β-strand | 127-133 | 7 | 7 |
| β-strand | 138 | 1 | 8 |
| α-helix | 139-148 | 10 | |
| α-helix | 152-154 | 3 | |
| α-helix | 155-173 | 19 | |
| β-strand | 177-178 | 2 | 9 |
| α-helix | 184-186 | 3 | |
| β-strand | 187-189 | 3 | 8 |
| β-strand | 196-198 | 3 | 8 |
| α-helix | 201-203 | 3 | |
| β-strand | 205-206 | 2 | 9 |
| α-helix | 220-222 | 3 | |
| α-helix | 225-228 | 4 | |
| α-helix | 237-252 | 16 | |
| α-helix | 264-273 | 10 | |
| α-helix | 276-277 | 2 | |
| α-helix | 278-284 | 7 | |
| 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 | |
| α-helix | 380-382 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 38-44 | 7 | 10 |
| β-strand | 52-64 | 13 | 10 |
| β-strand | 69-75 | 7 | 10 |
| β-strand | 81-87 | 7 | 10 |
| α-helix | 96-102 | 7 | |
| β-strand | 109 | 1 | 11 |
| β-strand | 112-117 | 6 | 10 |
| β-strand | 128-133 | 6 | 10 |
| β-strand | 137-138 | 2 | 11 |
| α-helix | 139-147 | 9 | |
| α-helix | 155-174 | 20 | |
| β-strand | 177-178 | 2 | 12 |
| α-helix | 184-186 | 3 | |
| β-strand | 187-190 | 4 | 11 |
| β-strand | 195-198 | 4 | 11 |
| α-helix | 201-203 | 3 | |
| β-strand | 205-206 | 2 | 12 |
| α-helix | 220-222 | 3 | |
| α-helix | 225-228 | 4 | |
| α-helix | 237-252 | 16 | |
| α-helix | 264-273 | 10 | |
| α-helix | 275-277 | 3 | |
| α-helix | 278-283 | 6 | |
| α-helix | 297-300 | 4 | |
| α-helix | 301-304 | 4 | |
| α-helix | 306 | 1 | |
| α-helix | 311-318 | 8 | |
| 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 | |
| β-strand | 349 | 1 | 13 |
| β-strand | 355 | 1 | 13 |
| α-helix | 356-357 | 2 | |
| α-helix | 364-367 | 4 | |
| α-helix | 371-373 | 3 | |
| α-helix | 374-377 | 4 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Glycogen synthase kinase-3 beta | A, B, C, D | protein | 420 | Mus musculus | Q9WV60 (AlphaFold model) |
>6AE3_1 Glycogen synthase kinase-3 beta (chains A, B, C, D) MSGRPRTTSFAESCKPVQQPSAFGSMKVSRDKDGSKVTTVVATPGQGPDRPQEVSYTDTK VIGNGSFGVVYQAKLCDSGELVAIKKVLQDKRFKNRELQIMRKLDHCNIVRLRYFFYSSG EKKDEVYLNLVLDYVPETVYRVARHYSRAKQTLPVIYVKLYMYQLFRSLAYIHSFGICHR DIKPQNLLLDPDTAVLKLCDFGSAKQLVRGEPNVSYICSRYYRAPELIFGATDYTSSIDV WSAGCVLAELLLGQPIFPGDSGVDQLVEIIKVLGTPTREQIREMNPNYTEFKFPQIKAHP WTKVFRPRTPPEAIALCSRLLEYTPTARLTPLEACAHSFFDELRDPNVKLPNGRDTPALF NFTTQELSSNPPLATILIPPHARIQAAASPPANATAASDTNAGDRGQTNNAASASASNST
| ID | Name | Formula | Copies |
|---|---|---|---|
| MRI | 2-[2,4-bis(oxidanyl)phenyl]-3,5,7-tris(oxidanyl)chromen-4-one | C15 H10 O7 | 2 |
Water and common crystallization additives (GOL) are not listed.
Crystal structure of GSK3 beta in complex with the flavonoid, morin. Kim, K., Cha, J.S., Kim, J.S. et al. Biochem Biophys Res Commun (2018) 504:519-524. DOI 10.1016/j.bbrc.2018.08.182 · PubMed
Other PDB entries of the same protein (UniProt Q9WV60 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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