9S8K: Glycogen phosphorylase - tetrameric form -

Structure of glycogen phosphorylase - tetrameric form - in complex with HPr from Escherichia coli. Determined by electron microscopy at 2.06 Å resolution. Released 8 Apr 2026.

Method: Electron microscopy
Resolution: 2.06 Å
Organism: Escherichia coli
Chains: 8
Atoms: 28,332
Mol. weight: 427.01 kDa
Released: 8 Apr 2026

Explore 9S8K in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

9S8K contains 217 α-helices and 110 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.

Chain A: 52 helices, 24 β-strands

Element	Residues	Length	Sheet
α-helix	13-23	11
α-helix	24-28	5
α-helix	38-67	30
β-strand	71-75	5	1
α-helix	85-92	8
α-helix	95-104	10
α-helix	109-115	7
α-helix	116-119	4
α-helix	125-140	16
β-strand	144-149	6	1
β-strand	154-161	8	2
β-strand	164-170	7	2
β-strand	181-192	12	1
β-strand	195-199	5	3
β-strand	202-206	5	3
β-strand	209-221	13	1
α-helix	222	1
β-strand	228-238	11	1
α-helix	242-245	4
α-helix	252-256	5
α-helix	262-266	5
α-helix	276-305	30
α-helix	311-314	4
β-strand	315-320	6	1
α-helix	323-326	4
α-helix	327-339	13
α-helix	343-353	11
β-strand	354-357	4	1
α-helix	363-365	3
β-strand	368-370	3	4
α-helix	371-377	7
α-helix	379-399	21
α-helix	405-410	6
β-strand	413-414	2	4
β-strand	420-422	3	4
α-helix	423-430	8
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	470	1
α-helix	471-476	6
α-helix	479-489	11
α-helix	492-494	3
α-helix	497-501	5
α-helix	502	1
α-helix	503-507	5
α-helix	510-535	26
β-strand	544-549	6	6
α-helix	554-556	3
α-helix	558-574	17
α-helix	580-582	3
β-strand	583-588	6	6
α-helix	596-613	18
β-strand	622-627	6	6
α-helix	632-638	7
α-helix	639-641	3
β-strand	644-647	4	6
α-helix	649-650	2
α-helix	658-665	8
β-strand	669-672	4	6
α-helix	677-685	9
α-helix	687-689	3
β-strand	691-692	2	6
α-helix	697-705	9
α-helix	710-716	7
α-helix	718-729	12
α-helix	741-748	8
α-helix	760-775	16
α-helix	777-789	13
α-helix	792-794	3
β-strand	795	1	5
α-helix	796-803	8
α-helix	804-808	5

Chain B: 52 helices, 24 β-strands

Element	Residues	Length	Sheet
α-helix	14-23	10
α-helix	24-29	6
α-helix	38-67	30
β-strand	71-75	5	7
α-helix	85-92	8
α-helix	95-104	10
α-helix	109-113	5
α-helix	117-119	3
α-helix	125-140	16
β-strand	144-149	6	7
β-strand	154-161	8	8
β-strand	164-170	7	8
β-strand	181-192	12	7
β-strand	195-199	5	9
β-strand	202-206	5	9
β-strand	209-221	13	7
α-helix	222	1
β-strand	228-237	10	7
α-helix	242-245	4
α-helix	252-255	4
α-helix	262-266	5
α-helix	270-271	2
α-helix	276-305	30
α-helix	311-314	4
β-strand	315-320	6	7
α-helix	323-326	4
α-helix	327-339	13
α-helix	343-353	11
β-strand	354-357	4	7
α-helix	363-365	3
β-strand	368-370	3	10
α-helix	371-377	7
α-helix	379-399	21
α-helix	405-410	6
β-strand	413-414	2	10
β-strand	420-422	3	10
α-helix	423-430	8
β-strand	433-436	4	7
α-helix	439-444	6
α-helix	445-449	5
α-helix	451-456	6
α-helix	458-460	3
β-strand	461-463	3	7
β-strand	468	1	11
α-helix	470	1
α-helix	471-476	6
α-helix	479-489	11
α-helix	492-494	3
α-helix	497-501	5
α-helix	502-505	4
α-helix	510-535	26
β-strand	544-549	6	12
α-helix	558-574	17
α-helix	580-582	3
β-strand	583-588	6	12
α-helix	590-592	3
α-helix	596-613	18
α-helix	619-621	3
β-strand	622-627	6	12
α-helix	632-638	7
α-helix	639-641	3
β-strand	644-647	4	12
α-helix	649-650	2
α-helix	659-665	7
β-strand	669-672	4	12
α-helix	677-685	9
β-strand	691-692	2	12
α-helix	697-706	10
α-helix	710-716	7
α-helix	718-728	11
α-helix	741-748	8
α-helix	760-775	16
α-helix	777-789	13
α-helix	792-794	3
β-strand	795	1	11
α-helix	796-806	11

Chain C: 50 helices, 24 β-strands

Element	Residues	Length	Sheet
α-helix	14-23	10
α-helix	24-29	6
α-helix	38-67	30
β-strand	71-75	5	13
α-helix	85-92	8
α-helix	95-103	9
α-helix	109-115	7
α-helix	116-119	4
α-helix	125-140	16
β-strand	144-149	6	13
β-strand	154-161	8	14
β-strand	164-170	7	14
β-strand	181-192	12	13
β-strand	195-199	5	15
β-strand	202-206	5	15
β-strand	209-221	13	13
α-helix	222	1
β-strand	228-237	10	13
α-helix	242-245	4
α-helix	252-255	4
α-helix	262-266	5
α-helix	276-305	30
β-strand	315-320	6	13
α-helix	323-326	4
α-helix	327-333	7
α-helix	334-338	5
α-helix	343-353	11
β-strand	354-357	4	13
α-helix	363-365	3
β-strand	368-370	3	16
α-helix	371-377	7
α-helix	379-399	21
α-helix	405-410	6
β-strand	413-414	2	16
β-strand	420-422	3	16
α-helix	423-430	8
β-strand	433-436	4	13
α-helix	439-444	6
α-helix	445-449	5
α-helix	451-456	6
α-helix	458-460	3
β-strand	461-463	3	13
β-strand	468	1	17
α-helix	470	1
α-helix	471-476	6
α-helix	479-489	11
α-helix	492-494	3
α-helix	497-500	4
α-helix	501-504	4
α-helix	510-535	26
β-strand	544-549	6	18
α-helix	558-574	17
β-strand	583-588	6	18
α-helix	590-592	3
α-helix	596-613	18
α-helix	619-621	3
β-strand	622-627	6	18
α-helix	632-638	7
α-helix	639-641	3
β-strand	644-647	4	18
α-helix	649-650	2
α-helix	659-665	7
β-strand	669-672	4	18
α-helix	678-685	8
β-strand	691-692	2	18
α-helix	697-706	10
α-helix	710-716	7
α-helix	718-728	11
α-helix	741-748	8
α-helix	760-775	16
α-helix	777-788	12
α-helix	792-794	3
β-strand	795	1	17
α-helix	796-806	11

Chain D: 51 helices, 22 β-strands

Element	Residues	Length	Sheet
α-helix	14-23	10
α-helix	24-28	5
α-helix	38-67	30
β-strand	71-75	5	19
α-helix	85-92	8
α-helix	95-104	10
α-helix	109-115	7
α-helix	116-119	4
α-helix	125-140	16
β-strand	144-149	6	19
α-helix	156	1
β-strand	157-161	5	20
β-strand	164-168	5	20
β-strand	181-199	19	19
β-strand	202-221	20	19
β-strand	228-238	11	19
α-helix	242-245	4
α-helix	252-255	4
α-helix	262-266	5
α-helix	276-305	30
α-helix	311-314	4
β-strand	315-320	6	19
α-helix	323-326	4
α-helix	327-339	13
α-helix	343-353	11
β-strand	354-357	4	19
α-helix	363-365	3
β-strand	368-370	3	21
α-helix	371-377	7
α-helix	379-399	21
α-helix	405-409	5
β-strand	413-414	2	21
β-strand	420-422	3	21
α-helix	423-430	8
β-strand	433-436	4	19
α-helix	439-444	6
α-helix	445-449	5
α-helix	451-456	6
β-strand	461-463	3	19
β-strand	468	1	22
α-helix	470	1
α-helix	471-476	6
α-helix	479-489	11
α-helix	492-494	3
α-helix	497-501	5
α-helix	502-505	4
α-helix	509-535	27
β-strand	544-549	6	23
α-helix	554-556	3
α-helix	558-574	17
α-helix	580-582	3
β-strand	583-588	6	23
α-helix	590-592	3
α-helix	596-612	17
α-helix	619-621	3
β-strand	622-627	6	23
α-helix	632-638	7
α-helix	639-641	3
β-strand	644-647	4	23
α-helix	649-650	2
α-helix	659-665	7
β-strand	669-672	4	23
α-helix	677-685	9
β-strand	691-692	2	23
α-helix	697-705	9
α-helix	710-716	7
α-helix	718-729	12
α-helix	741-748	8
α-helix	760-775	16
α-helix	777-789	13
α-helix	792-794	3
β-strand	795	1	22
α-helix	796-806	11

Chains E and F: 3 helices, 4 β-strands

Element	Residues	Length	Sheet
β-strand	2-7	6	24
α-helix	16-27	12
β-strand	32-37	6	24
β-strand	40-43	4	24
α-helix	47-50	4
β-strand	60-66	7	24
α-helix	72-83	12

Chain G: 3 helices, 4 β-strands

Element	Residues	Length	Sheet
β-strand	2-7	6	26
α-helix	16-26	11
β-strand	32-37	6	26
β-strand	40-43	4	26
α-helix	47-51	5
β-strand	60-66	7	26
α-helix	70-82	13

Chain H: 3 helices, 4 β-strands

Element	Residues	Length	Sheet
β-strand	3-7	5	27
α-helix	16-28	13
β-strand	32-37	6	27
β-strand	40-43	4	27
α-helix	47-51	5
β-strand	60-66	7	27
α-helix	70-83	14

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Glycogen phosphorylase	A	protein	832	Escherichia coli	P0AC86 (AlphaFold model)
Glycogen phosphorylase	B, C, D	protein	832	Escherichia coli	P0AC86 (AlphaFold model)
Phosphocarrier protein HPr	E, F, G, H	protein	102	Escherichia coli	P0AA04 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>9S8K_1 Glycogen phosphorylase (chains A)
MHHHHHHENLYFQGSGAMNAPFTYSSPTLSVEALKHSIAYKLMFTIGKDPVVANKHEWLN
ATLFAVRDRLVERWLRSNRAQLSQETRQVYYLSMEFLIGRTLSNAMLSLGIYEDVQGALE
AMGLNLEELIDEENDPGLGNGGLGRLAACFLDSLATLGLPGRGYGIRYDYGMFKQNIVNG
SQKESPDYWLEYGNPWEFKRHNTRYKVRFGGRIQQEGKKTRWIETEEILGVAYDQIIPGY
DTDATNTLRLWSAQASSEINLGKFNQGDYFAAVEDKNHSENVSRVLYPDDSTYSGRELRL
RQEYFLVSSTIQDILSRHYQLHKTYDNLADKIAIHLNDTHPVLSIPEMMRLLIDEHQFSW
DDAFEVCCQVFSYTNHTLMSEALETWPVDMLGKILPRHLQIIFEINDYFLKTLQEQYPND
TDLLGRASIIDESNGRRVRMAWLAVVVSHKVNGVSELHSNLMVQSLFADFAKIFPGRFTN
VTNGVTPRRWLAVANPSLSAVLDEHLGRNWRTDLSLLNELQQHCDFPMVNHAVHQAKLEN
KKRLAEYIAQQLNVVVNPKALFDVQIKRIHEYKRQLMNVLHVITRYNRIKADPDAKWVPR
VNIFGGKAASAYYMAKHIIHLINDVAKVINNDPQIGDKLKVVFIPNYSVSLAQLIIPAAD
LSEQISLAGTEASGTSNMKFALNGALTIGTLDGANVEMLDHVGADNIFIFGNTAEEVEEL
RRQGYKPREYYEKDEELHQVLTQIGSGVFSPEDPGRYRDLVDSLINFGDHYQVLADYRSY
VDCQDKVDELYELQEEWTAKAMLNIANMGYFSSDRTIKEYADHIWHIDPVRL

Sequence of entity 2 (B, C, D), FASTA

>9S8K_2 Glycogen phosphorylase (chains B, C, D)
MHHHHHHENLYFQGSGAMNAPFTYSSPTLSVEALKHSIAYKLMFTIGKDPVVANKHEWLN
ATLFAVRDRLVERWLRSNRAQLSQETRQVYYLSMEFLIGRTLSNAMLSLGIYEDVQGALE
AMGLNLEELIDEENDPGLGNGGLGRLAACFLDSLATLGLPGRGYGIRYDYGMFKQNIVNG
SQKESPDYWLEYGNPWEFKRHNTRYKVRFGGRIQQEGKKTRWIETEEILGVAYDQIIPGY
DTDATNTLRLWSAQASSEINLGKFNQGDYFAAVEDKNHSENVSRVLYPDDSTYSGRELRL
RQEYFLVSSTIQDILSRHYQLHKTYDNLADKIAIHLNDTHPVLSIPEMMRLLIDEHQFSW
DDAFEVCCQVFSYTNHTLMSEALETWPVDMLGKILPRHLQIIFEINDYFLKTLQEQYPND
TDLLGRASIIDESNGRRVRMAWLAVVVSHKVNGVSELHSNLMVQSLFADFAKIFPGRFTN
VTNGVTPRRWLAVANPSLSAVLDEHLGRNWRTDLSLLNELQQHCDFPMVNHAVHQAKLEN
KKRLAEYIAQQLNVVVNPKALFDVQIKRIHEYKRQLMNVLHVITRYNRIKADPDAKWVPR
VNIFGGKAASAYYMAKHIIHLINDVAKVINNDPQIGDKLKVVFIPNYSVSLAQLIIPAAD
LSEQISLAGTEASGTSNMKFALNGALTIGTLDGANVEMLDHVGADNIFIFGNTAEEVEEL
RRQGYKPREYYEKDEELHQVLTQIGSGVFSPEDPGRYRDLVDSLINFGDHYQVLADYRSY
VDCQDKVDELYELQEEWTAKAMLNIANMGYFSSDRTIKEYADHIWHIDPVRL

Sequence of entity 3 (E, F, G, H), FASTA

>9S8K_3 Phosphocarrier protein HPr (chains E, F, G, H)
MHHHHHHENLYFQGSGAMFQQEVTITAPNGLHTRPAAQFVKEAKGFTSEITVTSNGKSAS
AKSLFKLQTLGLTQGTVVTISAEGEDEQKAVEHLVKLMAELE

Primary citation

Structural basis for phosphorylation and allosteric regulation of bacterial glycogen phosphorylase by histidine phosphocarrier protein. Di Domenico, V., Franceus, J., Mastrella, L. et al. Nat Commun (2026) 17. DOI 10.1038/s41467-026-71729-w · PubMed

Other PDB entries of the same protein (UniProt P0AC86 (AlphaFold model), which also has an AlphaFold model), best resolution first:

9S8B 2.79 Å, Structure of glycogen phosphorylase - dimeric form - in complex with HPr from…
9M9P 2.93 Å, Glycogen phosphorylase dimer from E. coli
9S86 2.97 Å, Structure of glycogen phosphorylase - tetrameric form - from Escherichia coli
9S7V 3.1 Å, Structure of glycogen phosphorylase - dimeric form - from Escherichia coli
9V16 3.45 Å, Crystal structure of E. coli glycogen phosphorylase N185A/R267E mutant in complex with AMP
9UKQ 3.5 Å, Crystal structure of glycogen phosphorylase from Escherichia coli
9UKR 3.55 Å, Crystal structure of glycogen phosphorylase from E. coli in complex with AMP
9V17 3.7 Å, Crystal structure of E. coli glycogen phosphorylase N185A/R267E mutant

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