Crystal structure of GSK-3 26-383 bound to Axin 383-435. Determined by X-ray diffraction at 2.45 Å resolution. Released 28 Aug 2024.
Explore 8VMG in 3D Show helices and sheets RCSB PDB PDBe
8VMG contains 51 α-helices and 25 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 | 27-30 | 4 | 1 |
| β-strand | 36-44 | 9 | 1 |
| β-strand | 52-65 | 14 | 1 |
| β-strand | 68-75 | 8 | 1 |
| β-strand | 81-88 | 8 | 1 |
| α-helix | 97-103 | 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 | 155-174 | 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 |
| α-helix | 220-222 | 3 | |
| α-helix | 225-228 | 4 | |
| α-helix | 237-252 | 16 | |
| α-helix | 262-273 | 12 | |
| α-helix | 275-277 | 3 | |
| α-helix | 278-284 | 7 | |
| α-helix | 286-288 | 3 | |
| α-helix | 296-300 | 5 | |
| 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 | 338-340 | 3 | |
| α-helix | 341-344 | 4 | |
| α-helix | 355-356 | 2 | |
| α-helix | 371-373 | 3 | |
| α-helix | 374-377 | 4 | |
| α-helix | 380-383 | 4 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 37-44 | 8 | 4 |
| β-strand | 52-65 | 14 | 4 |
| β-strand | 68-75 | 8 | 4 |
| β-strand | 81-88 | 8 | 4 |
| α-helix | 96-103 | 8 | |
| β-strand | 109 | 1 | 5 |
| β-strand | 112-119 | 8 | 4 |
| β-strand | 126-133 | 8 | 4 |
| β-strand | 137-138 | 2 | 5 |
| α-helix | 139-148 | 10 | |
| α-helix | 152-154 | 3 | |
| α-helix | 155-174 | 20 | |
| β-strand | 177-178 | 2 | 6 |
| α-helix | 184-186 | 3 | |
| β-strand | 187-189 | 3 | 5 |
| β-strand | 196-198 | 3 | 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 | 262-273 | 12 | |
| α-helix | 276-277 | 2 | |
| α-helix | 278-284 | 7 | |
| α-helix | 286-288 | 3 | |
| α-helix | 296-300 | 5 | |
| 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 | 354-356 | 3 | |
| α-helix | 364-367 | 4 | |
| α-helix | 371-373 | 3 | |
| α-helix | 374-377 | 4 | |
| α-helix | 380-383 | 4 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 385-414 | 30 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 385-410 | 26 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Glycogen synthase kinase-3 beta | A, B | protein | 364 | Mus musculus | Q9WV60 (AlphaFold model) |
| Axin-1 | C, D | protein | 60 | Homo sapiens | O15169 (AlphaFold model) |
>8VMG_1 Glycogen synthase kinase-3 beta (chains A, B) MKVSRDKDGSKVTTVVATPGQGPDRPQEVSYTDTKVIGNGSFGVVYQAKLCDSGELVAIK KVLQDKRFKNRELQIMRKLDHCNIVRLRYFFYSSGEKKDEVYLNLVLDYVPETVYRVARH YSRAKQTLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDPDTAVLKLCDFGSAK QLVRGEPNVSYICSRYYRAPELIFGATDYTSSIDVWSAGCVLAELLLGQPIFPGDSGVDQ LVEIIKVLGTPTREQIREMNPNYTEFKFPQIKAHPWTKVFRPRTPPEAIALCSRLLEYTP TARLTPLEACAHSFFDELRDPNVKLPNGRDTPALFNFTTQELSSNPPLATILIPPHARHH HHHH
>8VMG_2 Axin-1 (chains C, D) GGWGSGGVEPQKFAEELIHRLEAVQRTREAEEKLEERLKRVRMEEEGEDGDPSSGPPGPC
Water and common crystallization additives (EDO, NO3, GOL, SO4, CL, MES) are not listed.
Structural and functional effects of phosphopriming and scaffolding in the kinase GSK-3 beta. Enos, M.D., Gavagan, M., Jameson, N. et al. Sci Signal (2024) 17. DOI 10.1126/scisignal.ado0881 · 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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