Glycogen synthase kinase-3 beta (GSK3) complex with FRATtide peptide. Determined by X-ray diffraction at 2.6 Å resolution. Released 3 Oct 2002.
Explore 1GNG in 3D Show helices and sheets RCSB PDB PDBe
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.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 38-44 | 7 | 1 |
| β-strand | 52-64 | 13 | 1 |
| β-strand | 69-75 | 7 | 1 |
| β-strand | 81-90 | 10 | 1 |
| α-helix | 96-103 | 8 | |
| β-strand | 109 | 1 | 2 |
| β-strand | 112-118 | 7 | 1 |
| β-strand | 125-133 | 9 | 1 |
| β-strand | 138 | 1 | 2 |
| α-helix | 139-148 | 10 | |
| α-helix | 155-174 | 20 | |
| β-strand | 177-178 | 2 | 3 |
| α-helix | 184-186 | 3 | |
| β-strand | 187-189 | 3 | 2 |
| β-strand | 196-198 | 3 | 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 | 276-277 | 2 | |
| 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 | 354-356 | 3 | |
| α-helix | 364-367 | 4 | |
| α-helix | 371-373 | 3 | |
| α-helix | 374-377 | 4 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 30 | 1 | 4 |
| β-strand | 36 | 1 | 4 |
| β-strand | 37-44 | 8 | 5 |
| β-strand | 52-63 | 12 | 5 |
| β-strand | 68-75 | 8 | 5 |
| β-strand | 81-90 | 10 | 5 |
| α-helix | 96-103 | 8 | |
| β-strand | 109 | 1 | 6 |
| β-strand | 112-119 | 8 | 5 |
| β-strand | 125-133 | 9 | 5 |
| β-strand | 138 | 1 | 6 |
| α-helix | 139-148 | 10 | |
| α-helix | 155-174 | 20 | |
| β-strand | 177-178 | 2 | 7 |
| α-helix | 184-186 | 3 | |
| β-strand | 187-189 | 3 | 6 |
| β-strand | 196-198 | 3 | 6 |
| β-strand | 205-206 | 2 | 7 |
| α-helix | 220-222 | 3 | |
| α-helix | 225-228 | 4 | |
| α-helix | 237-252 | 16 | |
| α-helix | 262-273 | 12 | |
| 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 | 354-356 | 3 | |
| α-helix | 364-367 | 4 | |
| α-helix | 371-373 | 3 | |
| α-helix | 374-377 | 4 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 199-209 | 11 | |
| α-helix | 212-221 | 10 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 199-209 | 11 | |
| α-helix | 212-220 | 9 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Glycogen synthase kinase-3 beta | A, B | protein | 378 | HOMO SAPIENS | P49841 (AlphaFold model) |
| Frattide | X, Y | protein | 39 | HOMO SAPIENS | Q92837 (AlphaFold model) |
>1GNG_1 GLYCOGEN SYNTHASE KINASE-3 BETA (chains A, B) MHHHHHHHHHHKVSRDKDGSKVTTVVATPGQGPDRPQEVSYTDTKVIGNGSFGVVYQAKL CDSGELVAIKKVLQDKRFKNRELQIMRKLDHCNIVRLRYFFYSSGEKKDEVYLNLVLDYV PETVYRVARHYSRAKQTLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDPDTAV LKLCDFGSAKQLVRGEPNVSYICSRYYRAPELIFGATDYTSSIDVWSAGCVLAELLLGQP IFPGDSGVDQLVEIIKVLGTPTREQIREMNPNYTEFKFPQIKAHPWTKVFRPRTPPEAIA LCSRLLEYTPTARLTPLEACAHSFFDELRDPNVKLPNGRDTPALFNFTTQELSSNPPLAT ILIPPHARIQAAASTPTN
>1GNG_2 FRATTIDE (chains X, Y) SQPETRTGDDDPHRLLQQLVLSGNLIKEAVRRLHSRRLQ
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:
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