Human GYS1-GYG1 complex activated state bound to glucose-6-phosphate. Determined by electron microscopy at 3.7 Å resolution. Released 27 Jul 2022.
Explore 7Q12 in 3D Show helices and sheets RCSB PDB PDBe
7Q12 contains 116 α-helices and 80 β-strands across 8 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 | 30-32 | 3 | 1 |
| α-helix | 43-58 | 16 | |
| β-strand | 63-68 | 6 | 1 |
| α-helix | 70-72 | 3 | |
| β-strand | 77-79 | 3 | 1 |
| α-helix | 83 | 1 | |
| β-strand | 84 | 1 | 2 |
| β-strand | 87 | 1 | 2 |
| α-helix | 89-96 | 8 | |
| β-strand | 101-106 | 6 | 1 |
| β-strand | 113-118 | 6 | 1 |
| α-helix | 126-131 | 6 | |
| α-helix | 146-168 | 23 | |
| β-strand | 175-179 | 5 | 1 |
| α-helix | 186-193 | 8 | |
| β-strand | 198-204 | 7 | 1 |
| α-helix | 208-213 | 6 | |
| α-helix | 221-223 | 3 | |
| α-helix | 229-234 | 6 | |
| α-helix | 239-251 | 13 | |
| β-strand | 254-257 | 4 | 1 |
| α-helix | 260-270 | 11 | |
| β-strand | 276-277 | 2 | 1 |
| α-helix | 292-311 | 20 | |
| α-helix | 320-322 | 3 | |
| β-strand | 323-328 | 6 | 3 |
| α-helix | 339-353 | 15 | |
| β-strand | 361-366 | 6 | 3 |
| β-strand | 372-375 | 4 | 4 |
| α-helix | 377-410 | 34 | |
| α-helix | 424-435 | 12 | |
| α-helix | 440-442 | 3 | |
| β-strand | 444 | 1 | 3 |
| β-strand | 446-448 | 3 | 4 |
| α-helix | 455-463 | 9 | |
| β-strand | 473-477 | 5 | 3 |
| α-helix | 493-499 | 7 | |
| β-strand | 502-504 | 3 | 3 |
| α-helix | 515-522 | 8 | |
| β-strand | 526-529 | 4 | 3 |
| α-helix | 533-539 | 7 | |
| β-strand | 550-553 | 4 | 3 |
| α-helix | 560-576 | 17 | |
| α-helix | 579-590 | 12 | |
| α-helix | 593-596 | 4 | |
| α-helix | 598-616 | 19 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 319-321 | 3 | |
| α-helix | 323-325 | 3 | |
| α-helix | 339-345 | 7 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Glycogen [starch] synthase, muscle | A, B, C, D | protein | 737 | Homo sapiens | P13807 (AlphaFold model) |
| Glycogenin-1 | E, F, G, H | protein | 350 | Homo sapiens | P46976 (AlphaFold model) |
>7Q12_1 Glycogen [starch] synthase, muscle (chains A, B, C, D) MPLNRTLSMSSLPGLEDWEDEFDLENAVLFEVAWEVANKVGGIYTVLQTKAKVTGDEWGD NYFLVGPYTEQGVRTQVELLEAPTPALKRTLDSMNSKGCKVYFGRWLIEGGPLVVLLDVG ASAWALERWKGELWDTCNIGVPWYDREANDAVLFGFLTTWFLGEFLAQSEEKPHVVAHFH EWLAGVGLCLCRARRLPVATIFTTHATLLGRYLCAGAVDFYNNLENFNVDKEAGERQIYH RYCMERAAAHCAHVFTTVSQITAIEAQHLLKRKPDIVTPNGLNVKKFSAMHEFQNLHAQS KARIQEFVRGHFYGHLDFNLDKTLYFFIAGRYEFSNKGADVFLEALARLNYLLRVNGSEQ TVVAFFIMPARTNNFNVETLKGQAVRKQLWDTANTVKEKFGRKLYESLLVGSLPDMNKML DKEDFTMMKRAIFATQRQSFPPVCTHNMLDDSSDPILTTIRRIGLFNSSADRVKVIFHPE FLSSTSPLLPVDYEEFVRGCHLGVFPSYYEPWGYTPAECTVMGIPSISTNLSGFGCFMEE HIADPSAYGIYILDRRFRSLDDSCSQLTSFLYSFCQQSRRQRIIQRNRTERLSDLLDWKY LGRYYMSARHMALSKAFPEHFTYEPNEADAAQGYRYPRPASVPPSPSLSRHSSPHQSEDE EDPRNGPLEEDGERYDEDEEAAKDRRNIRAPEWPRRASCTSSTSGSKRNSVDTATSSSLS TPSEPLSPTSSLGEERN
>7Q12_2 Glycogenin-1 (chains E, F, G, H) MTDQAFVTLTTNDAYAKGALVLGSSLKQHRTTRRLVVLATPQVSDSMRKVLETVFDEVIM VDVLDSGDSAHLTLMKRPELGVTLTKLHCWSLTQYSKCVFMDADTLVLANIDDLFDREEL SAAPDPGWPDCFNSGVFVYQPSVETYNQLLHLASEQGSFDGGDQGILNTFFSSWATTDIR KHLPFIYNLSSISIYSYLPAFKVFGASAKVVHFLGRVKPWNYTYDPKTKSVKSEAHDPNM THPEFLILWWNIFTTNVLPLLQQFGLVKDTCSYVNVLSDLVYTLAFSCGFCRKEDVSGAI SHLSLGEIPAMAQPFVSSEERKERWEQGQADYMGADSFDNIKRKLDTYLQ
| ID | Name | Formula | Copies |
|---|---|---|---|
| G6P | 6-O-phosphono-alpha-D-glucopyranose | C6 H13 O9 P | 4 |
Molecular basis for the regulation of human glycogen synthase by phosphorylation and glucose-6-phosphate. McCorvie, T.J., Loria, P.M., Tu, M. et al. Nat Struct Mol Biol (2022) 29:628-638. DOI 10.1038/s41594-022-00799-3 · PubMed
Other PDB entries of the same protein (UniProt P13807 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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