9M9P: Glycogen phosphorylase dimer from E. coli

Glycogen phosphorylase dimer from E. coli. Determined by electron microscopy at 2.93 Å resolution. Released 18 Feb 2026.

Method
Electron microscopy
Resolution
2.93 Å
Organism
Escherichia coli BL21(DE3)
Chains
1
Atoms
6,465
Mol. weight
95.55 kDa
Released
18 Feb 2026

Explore 9M9P in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

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.

Chain A: 44 helices, 26 β-strands

ElementResiduesLengthSheet
α-helix16-238
α-helix24-296
α-helix38-6629
β-strand71-7551
α-helix85-928
α-helix95-1039
α-helix109-1135
α-helix117-1182
α-helix124-14017
β-strand144-14961
β-strand157-16152
β-strand164-16852
β-strand180-192131
β-strand195-19953
β-strand202-20653
β-strand209-221131
β-strand228-238111
α-helix242-2454
α-helix252-2543
α-helix264-2663
α-helix279-30224
α-helix311-3144
β-strand315-31951
α-helix324-3263
α-helix327-33913
α-helix343-35311
β-strand354-35741
β-strand368-37034
α-helix371-3777
α-helix379-39921
α-helix404-4107
β-strand413-41424
β-strand420-42234
α-helix423-4297
β-strand433-43641
α-helix439-4446
α-helix445-4495
α-helix451-4566
β-strand461-46331
β-strand46815
α-helix479-48911
α-helix497-5048
α-helix509-53527
β-strand544-54966
β-strand55217
α-helix558-57417
α-helix580-5823
β-strand583-58866
α-helix5901
β-strand59117
α-helix5921
α-helix596-61217
β-strand622-62656
α-helix632-6387
α-helix639-6413
β-strand644-64746
α-helix649-6502
α-helix658-6669
β-strand669-67246
α-helix677-6859
β-strand691-69226
α-helix697-70610
α-helix710-7167
α-helix718-72912
α-helix741-7488
α-helix760-77415
α-helix777-78913
β-strand79515
α-helix796-8038
α-helix804-8085

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Alpha-1,4 glucan phosphorylaseAprotein832Escherichia coli BL21(DE3)P0AC86 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>9M9P_1 Alpha-1,4 glucan phosphorylase (chains A)
MGSSHHHHHHENLYFQGMNAPFTYSSPTLSVEALKHSIAYKLMFTIGKDPVVANKHEWLN
ATLFAVRDRLVERWLRSNRAQLSQETRQVYYLSMEFLIGRTLSNAMLSLGIYEDVQGALE
AMGLNLEELIDEENDPGLGNGGLGRLAACFLDSLATLGLPGRGYGIRYDYGMFKQNIVNG
SQKESPDYWLEYGNPWEFKRHNTRYKVRFGGRIQQEGKKTRWIETEEILGVAYDQIIPGY
DTDATNTLRLWSAQASSEINLGKFNQGDYFAAVEDKNHSENVSRVLYPDDSTYSGRELRL
RQEYFLVSSTIQDILSRHYQLHKTYDNLADKIAIHLNDTHPVLSIPEMMRLLIDEHQFSW
DDAFEVCCQVFSYTNHTLMSEALETWPVDMLGKILPRHLQIIFEINDYFLKTLQEQYPND
TDLLGRASIIDESNGRRVRMAWLAVVVSHKVNGVSELHSNLMVQSLFADFAKIFPGRFTN
VTNGVTPRRWLAVANPSLSAVLDEHLGRNWRTDLSLLNELQQHCDFPMVNHAVHQAKLEN
KKRLAEYIAQQLNVVVNPKALFDVQIKRIHEYKRQLMNVLHVITRYNRIKADPDAKWVPR
VNIFGGKAASAYYMAKHIIHLINDVAKVINNDPQIGDKLKVVFIPNYSVSLAQLIIPAAD
LSEQISLAGTEASGTSNMKFALNGALTIGTLDGANVEMLDHVGADNIFIFGNTAEEVEEL
RRQGYKPREYYEKDEELHQVLTQIGSGVFSPEDPGRYRDLVDSLINFGDHYQVLADYRSY
VDCQDKVDELYELQEEWTAKAMLNIANMGYFSSDRTIKEYADHIWHIDPVRL

Primary citation

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:

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