Glycogen phosphorylase dimer from E. coli. Determined by electron microscopy at 2.93 Å resolution. Released 18 Feb 2026.
Explore 9M9P in 3D Show helices and sheets RCSB PDB PDBe
9M9P contains 44 α-helices and 26 β-strands across 1 chain. 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 |
|---|---|---|---|
| α-helix | 16-23 | 8 | |
| α-helix | 24-29 | 6 | |
| α-helix | 38-66 | 29 | |
| β-strand | 71-75 | 5 | 1 |
| α-helix | 85-92 | 8 | |
| α-helix | 95-103 | 9 | |
| α-helix | 109-113 | 5 | |
| α-helix | 117-118 | 2 | |
| α-helix | 124-140 | 17 | |
| β-strand | 144-149 | 6 | 1 |
| β-strand | 157-161 | 5 | 2 |
| β-strand | 164-168 | 5 | 2 |
| β-strand | 180-192 | 13 | 1 |
| β-strand | 195-199 | 5 | 3 |
| β-strand | 202-206 | 5 | 3 |
| β-strand | 209-221 | 13 | 1 |
| β-strand | 228-238 | 11 | 1 |
| α-helix | 242-245 | 4 | |
| α-helix | 252-254 | 3 | |
| α-helix | 264-266 | 3 | |
| α-helix | 279-302 | 24 | |
| α-helix | 311-314 | 4 | |
| β-strand | 315-319 | 5 | 1 |
| α-helix | 324-326 | 3 | |
| α-helix | 327-339 | 13 | |
| α-helix | 343-353 | 11 | |
| β-strand | 354-357 | 4 | 1 |
| β-strand | 368-370 | 3 | 4 |
| α-helix | 371-377 | 7 | |
| α-helix | 379-399 | 21 | |
| α-helix | 404-410 | 7 | |
| β-strand | 413-414 | 2 | 4 |
| β-strand | 420-422 | 3 | 4 |
| α-helix | 423-429 | 7 | |
| β-strand | 433-436 | 4 | 1 |
| α-helix | 439-444 | 6 | |
| α-helix | 445-449 | 5 | |
| α-helix | 451-456 | 6 | |
| β-strand | 461-463 | 3 | 1 |
| β-strand | 468 | 1 | 5 |
| α-helix | 479-489 | 11 | |
| α-helix | 497-504 | 8 | |
| α-helix | 509-535 | 27 | |
| β-strand | 544-549 | 6 | 6 |
| β-strand | 552 | 1 | 7 |
| α-helix | 558-574 | 17 | |
| α-helix | 580-582 | 3 | |
| β-strand | 583-588 | 6 | 6 |
| α-helix | 590 | 1 | |
| β-strand | 591 | 1 | 7 |
| α-helix | 592 | 1 | |
| α-helix | 596-612 | 17 | |
| β-strand | 622-626 | 5 | 6 |
| α-helix | 632-638 | 7 | |
| α-helix | 639-641 | 3 | |
| β-strand | 644-647 | 4 | 6 |
| α-helix | 649-650 | 2 | |
| α-helix | 658-666 | 9 | |
| β-strand | 669-672 | 4 | 6 |
| α-helix | 677-685 | 9 | |
| β-strand | 691-692 | 2 | 6 |
| α-helix | 697-706 | 10 | |
| α-helix | 710-716 | 7 | |
| α-helix | 718-729 | 12 | |
| α-helix | 741-748 | 8 | |
| α-helix | 760-774 | 15 | |
| α-helix | 777-789 | 13 | |
| β-strand | 795 | 1 | 5 |
| α-helix | 796-803 | 8 | |
| α-helix | 804-808 | 5 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Alpha-1,4 glucan phosphorylase | A | protein | 832 | Escherichia coli BL21(DE3) | P0AC86 (AlphaFold model) |
>9M9P_1 Alpha-1,4 glucan phosphorylase (chains A) MGSSHHHHHHENLYFQGMNAPFTYSSPTLSVEALKHSIAYKLMFTIGKDPVVANKHEWLN ATLFAVRDRLVERWLRSNRAQLSQETRQVYYLSMEFLIGRTLSNAMLSLGIYEDVQGALE AMGLNLEELIDEENDPGLGNGGLGRLAACFLDSLATLGLPGRGYGIRYDYGMFKQNIVNG SQKESPDYWLEYGNPWEFKRHNTRYKVRFGGRIQQEGKKTRWIETEEILGVAYDQIIPGY DTDATNTLRLWSAQASSEINLGKFNQGDYFAAVEDKNHSENVSRVLYPDDSTYSGRELRL RQEYFLVSSTIQDILSRHYQLHKTYDNLADKIAIHLNDTHPVLSIPEMMRLLIDEHQFSW DDAFEVCCQVFSYTNHTLMSEALETWPVDMLGKILPRHLQIIFEINDYFLKTLQEQYPND TDLLGRASIIDESNGRRVRMAWLAVVVSHKVNGVSELHSNLMVQSLFADFAKIFPGRFTN VTNGVTPRRWLAVANPSLSAVLDEHLGRNWRTDLSLLNELQQHCDFPMVNHAVHQAKLEN KKRLAEYIAQQLNVVVNPKALFDVQIKRIHEYKRQLMNVLHVITRYNRIKADPDAKWVPR VNIFGGKAASAYYMAKHIIHLINDVAKVINNDPQIGDKLKVVFIPNYSVSLAQLIIPAAD LSEQISLAGTEASGTSNMKFALNGALTIGTLDGANVEMLDHVGADNIFIFGNTAEEVEEL RRQGYKPREYYEKDEELHQVLTQIGSGVFSPEDPGRYRDLVDSLINFGDHYQVLADYRSY VDCQDKVDELYELQEEWTAKAMLNIANMGYFSSDRTIKEYADHIWHIDPVRL
Structural and mechanistic diversity of glycogen phosphorylases from gut bacteria. Shobu, K., Takai, M., Tanino, H. et al. Proc Natl Acad Sci U S A (2026) 123:e2518513123-e2518513123. DOI 10.1073/pnas.2518513123 · PubMed
Other PDB entries of the same protein (UniProt P0AC86 (AlphaFold model), which also has an AlphaFold model), best resolution first:
MolViewer shows 9M9P directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.