9V17: Glycogen phosphorylase

Crystal structure of E. coli glycogen phosphorylase N185A/R267E mutant. Determined by X-ray diffraction at 3.7 Å resolution. Released 18 Feb 2026.

Method: X-ray diffraction
Resolution: 3.7 Å
Organism: Escherichia coli K12
Chains: 4
Atoms: 25,758
Mol. weight: 374.51 kDa
Released: 18 Feb 2026

Explore 9V17 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

9V17 contains 195 α-helices and 96 β-strands across 4 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: 48 helices, 24 β-strands

Element	Residues	Length	Sheet
α-helix	12-23	12
α-helix	24-28	5
α-helix	33-35	3
α-helix	38-67	30
β-strand	71-75	5	1
α-helix	84-92	9
α-helix	95-105	11
α-helix	109-114	6
α-helix	117-119	3
α-helix	125-139	15
β-strand	144-149	6	1
β-strand	157-161	5	2
β-strand	164-168	5	2
α-helix	172-175	4
β-strand	180-192	13	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	263-266	4
α-helix	276-305	30
α-helix	311-314	4
β-strand	315-319	5	1
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	1
α-helix	363-365	3
β-strand	368-370	3	4
α-helix	371-377	7
α-helix	379-399	21
α-helix	406-410	5
β-strand	413-414	2	4
β-strand	420-422	3	4
α-helix	423-430	8
β-strand	434-435	2	1
α-helix	439-444	6
α-helix	445-449	5
α-helix	451-456	6
β-strand	461	1	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	497-506	10
α-helix	512-534	23
β-strand	544-549	6	6
α-helix	558-574	17
β-strand	583-588	6	6
α-helix	596-612	17
β-strand	622-627	6	6
α-helix	632-638	7
β-strand	644-647	4	6
α-helix	649-650	2
α-helix	659-665	7
β-strand	669-672	4	6
α-helix	678-685	8
α-helix	687-689	3
β-strand	691-692	2	6
α-helix	697-705	9
α-helix	710-715	6
α-helix	718-728	11
α-helix	741-748	8
α-helix	760-774	15
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: 51 helices, 24 β-strands

Element	Residues	Length	Sheet
α-helix	14-27	14
α-helix	33-35	3
α-helix	38-67	30
α-helix	69-70	2
β-strand	71-75	5	7
α-helix	84-92	9
α-helix	95-104	10
α-helix	109-113	5
α-helix	117-119	3
α-helix	125-139	15
β-strand	144-149	6	7
β-strand	157-161	5	8
β-strand	164-168	5	8
α-helix	172-175	4
β-strand	180-192	13	7
β-strand	195-196	2	9
β-strand	205-206	2	9
β-strand	209-221	13	7
β-strand	228-237	10	7
α-helix	259-263	5
α-helix	264-266	3
α-helix	276-305	30
α-helix	311-314	4
β-strand	315-319	5	7
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	7
β-strand	368-370	3	10
α-helix	371-377	7
α-helix	379-399	21
α-helix	406-410	5
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	497-506	10
α-helix	510-534	25
β-strand	544-549	6	12
α-helix	558-574	17
β-strand	583-588	6	12
α-helix	596-612	17
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	658-664	7
β-strand	669-673	5	12
α-helix	677-685	9
α-helix	687-689	3
β-strand	691-693	3	12
α-helix	697-705	9
α-helix	710-716	7
α-helix	718-728	11
α-helix	737-740	4
α-helix	741-748	8
α-helix	760-774	15
α-helix	778-789	12
α-helix	791-794	4
β-strand	795	1	11
α-helix	796-802	7
α-helix	803-807	5
α-helix	812-814	3

Chain C: 48 helices, 24 β-strands

Element	Residues	Length	Sheet
α-helix	12-23	12
α-helix	24-28	5
α-helix	33-35	3
α-helix	38-67	30
β-strand	71-75	5	13
α-helix	84-92	9
α-helix	95-104	10
α-helix	109-113	5
α-helix	117-119	3
α-helix	127-139	13
β-strand	144-149	6	13
β-strand	157-160	4	14
β-strand	165-168	4	14
α-helix	172-175	4
β-strand	180-192	13	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	228-238	11	13
α-helix	276-305	30
α-helix	311-314	4
β-strand	315-319	5	13
α-helix	323-326	4
α-helix	327-337	11
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	379-392	14
α-helix	396-399	4
α-helix	406-410	5
β-strand	413-414	2	16
β-strand	420-422	3	16
α-helix	423-430	8
β-strand	433-435	3	13
α-helix	439-444	6
α-helix	445-449	5
α-helix	451-456	6
α-helix	458-460	3
β-strand	461-462	2	13
β-strand	468	1	17
α-helix	470	1
α-helix	471-476	6
α-helix	479-489	11
α-helix	497-506	10
α-helix	510-534	25
β-strand	544-549	6	18
α-helix	558-574	17
β-strand	583-588	6	18
α-helix	596-612	17
β-strand	622-627	6	18
α-helix	632-638	7
β-strand	644-647	4	18
α-helix	649-650	2
α-helix	659-665	7
β-strand	669-674	6	18
α-helix	678-685	8
α-helix	687-689	3
β-strand	691-696	6	18
α-helix	697-705	9
α-helix	710-716	7
α-helix	720-728	9
α-helix	737-739	3
α-helix	741-748	8
α-helix	760-774	15
α-helix	777-789	13
α-helix	791-794	4
β-strand	795	1	17
α-helix	796-802	7
α-helix	803-808	6

Chain D: 48 helices, 24 β-strands

Element	Residues	Length	Sheet
α-helix	12-23	12
α-helix	24-28	5
α-helix	38-67	30
α-helix	69-70	2
β-strand	71-75	5	19
α-helix	84-91	8
α-helix	95-104	10
α-helix	109-113	5
α-helix	117-119	3
α-helix	125-139	15
β-strand	144-149	6	19
β-strand	157-161	5	20
β-strand	164-168	5	20
α-helix	172-175	4
β-strand	180-192	13	19
β-strand	195-199	5	21
β-strand	202-206	5	21
β-strand	209-221	13	19
β-strand	228-237	10	19
α-helix	264-266	3
α-helix	278-305	28
α-helix	311-314	4
β-strand	315-319	5	19
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	19
α-helix	363-365	3
β-strand	368-370	3	22
α-helix	371-377	7
α-helix	379-399	21
α-helix	406-409	4
β-strand	413-414	2	22
α-helix	415-417	3
β-strand	420-422	3	22
α-helix	423-430	8
β-strand	433-435	3	19
α-helix	439-444	6
α-helix	445-449	5
α-helix	451-456	6
β-strand	461-462	2	19
β-strand	468	1	23
α-helix	470	1
α-helix	471-476	6
α-helix	479-489	11
α-helix	491-494	4
α-helix	497-506	10
α-helix	510-535	26
β-strand	544-549	6	24
α-helix	558-573	16
β-strand	583-588	6	24
α-helix	596-612	17
α-helix	619-621	3
β-strand	622-627	6	24
α-helix	632-638	7
β-strand	644-647	4	24
α-helix	649-650	2
α-helix	658-665	8
β-strand	669-673	5	24
α-helix	677-685	9
β-strand	691-693	3	24
α-helix	697-705	9
α-helix	710-716	7
α-helix	718-728	11
α-helix	737-740	4
α-helix	741-748	8
α-helix	760-775	16
α-helix	777-789	13
α-helix	791-794	4
β-strand	795	1	23
α-helix	796-806	11

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Glycogen phosphorylase	A, B, C, D	protein	817	Escherichia coli K12	P0AC86 (AlphaFold model)

Sequence of entity 1 (A, B, C, D), FASTA

>9V17_1 Glycogen phosphorylase (chains A, B, C, D)
MGMNAPFTYSSPTLSVEALKHSIAYKLMFTIGKDPVVANKHEWLNATLFAVRDRLVERWL
RSNRAQLSQETRQVYYLSMEFLIGRTLSNAMLSLGIYEDVQGALEAMGLNLEELIDEEND
PGLGNGGLGRLAACFLDSLATLGLPGRGYGIRYDYGMFKQNIVNGSQKESPDYWLEYGNP
WEFKRHATRYKVRFGGRIQQEGKKTRWIETEEILGVAYDQIIPGYDTDATNTLRLWSAQA
SSEINLGKFNQGDYFAAVEDKNHSENVSEVLYPDDSTYSGRELRLRQEYFLVSSTIQDIL
SRHYQLHKTYDNLADKIAIHLNDTHPVLSIPEMMRLLIDEHQFSWDDAFEVCCQVFSYTN
HTLMSEALETWPVDMLGKILPRHLQIIFEINDYFLKTLQEQYPNDTDLLGRASIIDESNG
RRVRMAWLAVVVSHKVNGVSELHSNLMVQSLFADFAKIFPGRFTNVTNGVTPRRWLAVAN
PSLSAVLDEHLGRNWRTDLSLLNELQQHCDFPMVNHAVHQAKLENKKRLAEYIAQQLNVV
VNPKALFDVQIKRIHEYKRQLMNVLHVITRYNRIKADPDAKWVPRVNIFGGKAASAYYMA
KHIIHLINDVAKVINNDPQIGDKLKVVFIPNYSVSLAQLIIPAADLSEQISLAGTEASGT
SNMKFALNGALTIGTLDGANVEMLDHVGADNIFIFGNTAEEVEELRRQGYKPREYYEKDE
ELHQVLTQIGSGVFSPEDPGRYRDLVDSLINFGDHYQVLADYRSYVDCQDKVDELYELQE
EWTAKAMLNIANMGYFSSDRTIKEYADHIWHIDPVRL

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:

9S8K 2.06 Å, Structure of glycogen phosphorylase - tetrameric form - in complex with HPr from…
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

Browse structure collections

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