8VME: GSK-3/Axin complex

Crystal structure of the GSK-3/Axin complex bound to a phosphorylated beta-catenin T41A peptide. Determined by X-ray diffraction at 2.3 Å resolution. Released 28 Aug 2024.

Method
X-ray diffraction
Resolution
2.3 Å
Organisms
Mus musculus, Homo sapiens
Chains
3
Atoms
3,308
Mol. weight
48.37 kDa
Ligands
MG, ADP
Released
28 Aug 2024

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

Secondary structure: helices and β-sheets

8VME contains 24 α-helices and 17 β-strands across 3 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: 23 helices, 16 β-strands

ElementResiduesLengthSheet
β-strand28-3031
β-strand36-4491
β-strand52-64131
β-strand68-7581
β-strand81-8881
β-strand9312
α-helix97-1026
β-strand10913
β-strand112-11871
β-strand127-13371
β-strand137-13823
α-helix139-14911
α-helix155-17420
β-strand177-17824
α-helix184-1863
β-strand187-19043
β-strand195-19843
β-strand205-20624
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
β-strand34915
α-helix3541
β-strand35515
α-helix356-3583
α-helix364-3674
α-helix371-3733
α-helix374-3774
α-helix380-3823
Chain B: 1 helix, 0 β-strands
ElementResiduesLengthSheet
α-helix385-39915
Chain C: 0 helices, 1 β-strand
ElementResiduesLengthSheet
β-strand4612

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Glycogen synthase kinase-3 betaAprotein365Mus musculusQ9WV60 (AlphaFold model)
Axin-1Bprotein24Homo sapiensO15169 (AlphaFold model)
Catenin beta-1Cprotein28Homo sapiensP35222 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>8VME_1 Glycogen synthase kinase-3 beta (chains A)
QMKVSRDKDGSKVTTVVATPGQGPDRPQEVSYTDTKVIGNGSFGVVYQAKLCDSGELVAI
KKVLQDKRFKNRELQIMRKLDHCNIVRLRYFFYSSGEKKDEVYLNLVLDYVPETVYRVAR
HYSRAKQTLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDPDTAVLKLCDFGSA
KQLVRGEPNVSYICSRYYRAPELIFGATDYTSSIDVWSAGCVLAELLLGQPIFPGDSGVD
QLVEIIKVLGTPTREQIREMNPNYTEFKFPQIKAHPWTKVFRPRTPPEAIALCSRLLEYT
PTARLTPLEACAHSFFDELRDPNVKLPNGRDTPALFNFTTQELSSNPPLATILIPPHARH
HHHHH
Sequence of entity 2 (B), FASTA
>8VME_2 Axin-1 (chains B)
GGILVEPQKFAEELIHRLEAVQRT
Sequence of entity 3 (C), FASTA
>8VME_3 Catenin beta-1 (chains C)
MIHSGATATAPSLSGKGNPEEEDVDTSQ

Ligands and cofactors

IDNameFormulaCopies
MGMagnesium ionMg2
ADPAdenosine-5'-diphosphateC10 H15 N5 O10 P21

Water and common crystallization additives (NA, GOL) 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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