Crystal structure of monomeric glycogen synthase from Pyrococcus abyssi. Determined by X-ray diffraction at 2.6 Å resolution. Released 29 Dec 2010.
Explore 3L01 in 3D Show helices and sheets RCSB PDB PDBe
3L01 contains 49 α-helices and 42 β-strands across 2 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 | 2-6 | 5 | 1 |
| β-strand | 10 | 1 | 2 |
| β-strand | 13 | 1 | 2 |
| α-helix | 18-31 | 14 | |
| β-strand | 35-41 | 7 | 1 |
| β-strand | 49-56 | 8 | 1 |
| β-strand | 59-70 | 12 | 1 |
| β-strand | 73-79 | 7 | 1 |
| α-helix | 81-84 | 4 | |
| α-helix | 92-115 | 24 | |
| α-helix | 119-121 | 3 | |
| β-strand | 123-127 | 5 | 1 |
| α-helix | 129-131 | 3 | |
| α-helix | 132-142 | 11 | |
| β-strand | 146-150 | 5 | 1 |
| β-strand | 158-159 | 2 | 3 |
| α-helix | 161-165 | 5 | |
| α-helix | 169-171 | 3 | |
| β-strand | 176-177 | 2 | 3 |
| α-helix | 179-186 | 8 | |
| β-strand | 189-192 | 4 | 1 |
| α-helix | 195-200 | 6 | |
| α-helix | 202-205 | 4 | |
| α-helix | 206-208 | 3 | |
| β-strand | 212-214 | 3 | 1 |
| α-helix | 226-228 | 3 | |
| α-helix | 233-242 | 10 | |
| β-strand | 250-255 | 6 | 4 |
| β-strand | 258 | 1 | 5 |
| α-helix | 265-275 | 11 | |
| α-helix | 280-283 | 4 | |
| β-strand | 284-289 | 6 | 4 |
| β-strand | 292 | 1 | 5 |
| α-helix | 294-306 | 13 | |
| β-strand | 310-313 | 4 | 4 |
| α-helix | 316-318 | 3 | |
| α-helix | 319-326 | 8 | |
| β-strand | 331-334 | 4 | 4 |
| α-helix | 343-350 | 8 | |
| α-helix | 353 | 1 | |
| β-strand | 354-358 | 5 | 4 |
| α-helix | 362-366 | 5 | |
| β-strand | 373-375 | 3 | 4 |
| α-helix | 380-393 | 14 | |
| α-helix | 398-409 | 12 | |
| α-helix | 414-425 | 12 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 2-6 | 5 | 6 |
| β-strand | 10 | 1 | 7 |
| β-strand | 13 | 1 | 7 |
| α-helix | 18-31 | 14 | |
| β-strand | 35-41 | 7 | 6 |
| β-strand | 49-56 | 8 | 6 |
| β-strand | 59-70 | 12 | 6 |
| β-strand | 73-79 | 7 | 6 |
| α-helix | 81-84 | 4 | |
| α-helix | 92-115 | 24 | |
| α-helix | 119-121 | 3 | |
| β-strand | 123-127 | 5 | 6 |
| α-helix | 129-131 | 3 | |
| α-helix | 132-142 | 11 | |
| β-strand | 146-150 | 5 | 6 |
| β-strand | 158-159 | 2 | 8 |
| α-helix | 161-165 | 5 | |
| α-helix | 169-171 | 3 | |
| β-strand | 176-177 | 2 | 8 |
| α-helix | 179-186 | 8 | |
| β-strand | 189-192 | 4 | 6 |
| α-helix | 195-200 | 6 | |
| α-helix | 202-205 | 4 | |
| α-helix | 206-208 | 3 | |
| β-strand | 212-214 | 3 | 6 |
| α-helix | 226-228 | 3 | |
| α-helix | 233-242 | 10 | |
| β-strand | 250-255 | 6 | 9 |
| β-strand | 258 | 1 | 10 |
| α-helix | 265-275 | 11 | |
| α-helix | 279-282 | 4 | |
| β-strand | 284-289 | 6 | 9 |
| β-strand | 292 | 1 | 10 |
| α-helix | 294-306 | 13 | |
| β-strand | 310-313 | 4 | 9 |
| α-helix | 319-326 | 8 | |
| β-strand | 331-334 | 4 | 9 |
| α-helix | 343-350 | 8 | |
| α-helix | 353 | 1 | |
| β-strand | 354-358 | 5 | 9 |
| α-helix | 363-366 | 4 | |
| β-strand | 373-375 | 3 | 9 |
| α-helix | 380-393 | 14 | |
| α-helix | 398-409 | 12 | |
| α-helix | 414-425 | 12 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| GlgA glycogen synthase | A, B | protein | 428 | Pyrococcus abyssi | Q9V2J8 (AlphaFold model) |
>3L01_1 GlgA glycogen synthase (chains A, B) RHMKVLLLGFEFLPVKVGGLAEALTAISEALASLGHEVLVFTPSHGRFQGEEIGKIRVFG EEVQVKVSYEERGNLRIYRIGGGLLDSEDVYGPGWDGLIRKAVTFGRASVLLLNDLLREE PLPDVVHFHDWHTVFAGALIKKYFKIPAVFTIHRLNKSKLPAFYFHEAGLSELAPYPDID PEHTGGYIADIVTTVSRGYLIDEWGFFRNFEGKITYVFNGIDCSFWNESYLTGSRDERKK SLLSKFGMDEGVTFMFIGRFDRGQKGVDVLLKAIEILSSKKEFQEMRFIIIGKGDPELEG WARSLEEKHGNVKVITEMLSREFVRELYGSVDFVIIPSYFEPFGLVALEAMCLGAIPIAS AVGGLRDIITNETGILVKAGDPGELANAILKALELSRSDLSKFRENCKKRAMSFSWEKSA ERYVKAYA
Processivity and Subcellular Localization of Glycogen Synthase Depend on a Non-catalytic High Affinity Glycogen-binding Site. Diaz, A., Martinez-Pons, C., Fita, I. et al. J Biol Chem (2011) 286:18505-18514. DOI 10.1074/jbc.M111.236109 · PubMed
Other PDB entries of the same protein (UniProt Q9V2J8 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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