8VMG: GSK-3 26-383

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.

Method
X-ray diffraction
Resolution
2.45 Å
Organisms
Mus musculus, Homo sapiens
Chains
4
Atoms
6,672
Mol. weight
101.72 kDa
Ligands
ADP, MG
Released
28 Aug 2024

Explore 8VMG in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

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.

Chain A: 24 helices, 13 β-strands

ElementResiduesLengthSheet
β-strand27-3041
β-strand36-4491
β-strand52-65141
β-strand68-7581
β-strand81-8881
α-helix97-1037
β-strand10912
β-strand112-11981
β-strand126-13381
β-strand137-13822
α-helix139-14810
α-helix152-1543
α-helix155-17420
β-strand177-17823
α-helix184-1863
β-strand187-19042
β-strand195-19842
β-strand205-20623
α-helix220-2223
α-helix225-2284
α-helix237-25216
α-helix262-27312
α-helix275-2773
α-helix278-2847
α-helix286-2883
α-helix296-3005
α-helix301-3044
α-helix311-32010
α-helix325-3273
α-helix329-3302
α-helix331-3355
α-helix338-3403
α-helix341-3444
α-helix355-3562
α-helix371-3733
α-helix374-3774
α-helix380-3834
Chain B: 25 helices, 12 β-strands
ElementResiduesLengthSheet
β-strand37-4484
β-strand52-65144
β-strand68-7584
β-strand81-8884
α-helix96-1038
β-strand10915
β-strand112-11984
β-strand126-13384
β-strand137-13825
α-helix139-14810
α-helix152-1543
α-helix155-17420
β-strand177-17826
α-helix184-1863
β-strand187-18935
β-strand196-19835
α-helix201-2033
β-strand205-20626
α-helix220-2223
α-helix225-2284
α-helix237-25216
α-helix262-27312
α-helix276-2772
α-helix278-2847
α-helix286-2883
α-helix296-3005
α-helix301-3044
α-helix311-3188
α-helix325-3273
α-helix329-3302
α-helix331-3355
α-helix338-3447
α-helix354-3563
α-helix364-3674
α-helix371-3733
α-helix374-3774
α-helix380-3834
Chain C: 1 helix, 0 β-strands
ElementResiduesLengthSheet
α-helix385-41430
Chain D: 1 helix, 0 β-strands
ElementResiduesLengthSheet
α-helix385-41026

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Glycogen synthase kinase-3 betaA, Bprotein364Mus musculusQ9WV60 (AlphaFold model)
Axin-1C, Dprotein60Homo sapiensO15169 (AlphaFold model)
Sequence of entity 1 (A, B), FASTA
>8VMG_1 Glycogen synthase kinase-3 beta (chains A, B)
MKVSRDKDGSKVTTVVATPGQGPDRPQEVSYTDTKVIGNGSFGVVYQAKLCDSGELVAIK
KVLQDKRFKNRELQIMRKLDHCNIVRLRYFFYSSGEKKDEVYLNLVLDYVPETVYRVARH
YSRAKQTLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDPDTAVLKLCDFGSAK
QLVRGEPNVSYICSRYYRAPELIFGATDYTSSIDVWSAGCVLAELLLGQPIFPGDSGVDQ
LVEIIKVLGTPTREQIREMNPNYTEFKFPQIKAHPWTKVFRPRTPPEAIALCSRLLEYTP
TARLTPLEACAHSFFDELRDPNVKLPNGRDTPALFNFTTQELSSNPPLATILIPPHARHH
HHHH
Sequence of entity 2 (C, D), FASTA
>8VMG_2 Axin-1 (chains C, D)
GGWGSGGVEPQKFAEELIHRLEAVQRTREAEEKLEERLKRVRMEEEGEDGDPSSGPPGPC

Ligands and cofactors

IDNameFormulaCopies
ADPAdenosine-5'-diphosphateC10 H15 N5 O10 P21
MGMagnesium ionMg1

Water and common crystallization additives (EDO, NO3, GOL, SO4, CL, MES) are not listed.

Primary citation

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:

Browse structure collections

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