1GNG: Glycogen synthase kinase-3 beta

Glycogen synthase kinase-3 beta (GSK3) complex with FRATtide peptide. Determined by X-ray diffraction at 2.6 Å resolution. Released 3 Oct 2002.

Method
X-ray diffraction
Resolution
2.6 Å
Organism
HOMO SAPIENS
Chains
4
Atoms
6,227
Mol. weight
95.85 kDa
Released
3 Oct 2002

Explore 1GNG in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1GNG contains 45 α-helices and 26 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: 21 helices, 12 β-strands

ElementResiduesLengthSheet
β-strand38-4471
β-strand52-64131
β-strand69-7571
β-strand81-90101
α-helix96-1038
β-strand10912
β-strand112-11871
β-strand125-13391
β-strand13812
α-helix139-14810
α-helix155-17420
β-strand177-17823
α-helix184-1863
β-strand187-18932
β-strand196-19832
β-strand205-20623
α-helix220-2223
α-helix225-2284
α-helix237-25216
α-helix262-27312
α-helix276-2772
α-helix278-2847
α-helix297-3004
α-helix301-3044
α-helix311-32010
α-helix325-3273
α-helix329-3302
α-helix331-3355
α-helix338-3447
α-helix354-3563
α-helix364-3674
α-helix371-3733
α-helix374-3774
Chain B: 20 helices, 14 β-strands
ElementResiduesLengthSheet
β-strand3014
β-strand3614
β-strand37-4485
β-strand52-63125
β-strand68-7585
β-strand81-90105
α-helix96-1038
β-strand10916
β-strand112-11985
β-strand125-13395
β-strand13816
α-helix139-14810
α-helix155-17420
β-strand177-17827
α-helix184-1863
β-strand187-18936
β-strand196-19836
β-strand205-20627
α-helix220-2223
α-helix225-2284
α-helix237-25216
α-helix262-27312
α-helix278-2847
α-helix297-3004
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
Chain X: 2 helices, 0 β-strands
ElementResiduesLengthSheet
α-helix199-20911
α-helix212-22110
Chain Y: 2 helices, 0 β-strands
ElementResiduesLengthSheet
α-helix199-20911
α-helix212-2209

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Glycogen synthase kinase-3 betaA, Bprotein378HOMO SAPIENSP49841 (AlphaFold model)
FrattideX, Yprotein39HOMO SAPIENSQ92837 (AlphaFold model)
Sequence of entity 1 (A, B), FASTA
>1GNG_1 GLYCOGEN SYNTHASE KINASE-3 BETA (chains A, B)
MHHHHHHHHHHKVSRDKDGSKVTTVVATPGQGPDRPQEVSYTDTKVIGNGSFGVVYQAKL
CDSGELVAIKKVLQDKRFKNRELQIMRKLDHCNIVRLRYFFYSSGEKKDEVYLNLVLDYV
PETVYRVARHYSRAKQTLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDPDTAV
LKLCDFGSAKQLVRGEPNVSYICSRYYRAPELIFGATDYTSSIDVWSAGCVLAELLLGQP
IFPGDSGVDQLVEIIKVLGTPTREQIREMNPNYTEFKFPQIKAHPWTKVFRPRTPPEAIA
LCSRLLEYTPTARLTPLEACAHSFFDELRDPNVKLPNGRDTPALFNFTTQELSSNPPLAT
ILIPPHARIQAAASTPTN
Sequence of entity 2 (X, Y), FASTA
>1GNG_2 FRATTIDE (chains X, Y)
SQPETRTGDDDPHRLLQQLVLSGNLIKEAVRRLHSRRLQ

Primary citation

The Structure of Phosphorylated Gsk-3Beta Complexed with a Peptide, Frattide, that Inhibits Beta-Catenin Phosphorylation. Bax, B., Carter, P.S., Lewis, C. et al. Structure (2001) 9:1143. DOI 10.1016/S0969-2126(01)00679-7 · PubMed

Other PDB entries of the same protein (UniProt P49841 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

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