8Z0A: Human GYS1-GYG2 complex

Human GYS1-GYG2 complex (apo). Determined by electron microscopy at 2.84 Å resolution. Released 9 Apr 2025.

Method: Electron microscopy
Resolution: 2.84 Å
Organism: Homo sapiens
Chains: 8
Atoms: 20,668
Mol. weight: 568.78 kDa
Released: 9 Apr 2025

Explore 8Z0A in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

8Z0A contains 116 α-helices and 88 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.

Chains A and B: 26 helices, 22 β-strands

Element	Residues	Length	Sheet
β-strand	28-32	5	1
α-helix	43-58	16
β-strand	62-67	6	1
α-helix	70-76	7
β-strand	77-79	3	1
α-helix	85-96	12
β-strand	101-106	6	1
β-strand	113-117	5	1
α-helix	120-125	6
α-helix	126-136	11
α-helix	146-168	23
β-strand	175-180	6	1
α-helix	181-192	12
β-strand	198-204	7	1
α-helix	208-215	8
α-helix	229-236	8
α-helix	239-251	13
β-strand	254-257	4	1
α-helix	260-269	10
β-strand	276-277	2	1
β-strand	282	1	2
α-helix	295-311	17
α-helix	320-322	3
β-strand	323-329	7	3
α-helix	339-355	17
β-strand	361-367	7	3
β-strand	372-375	4	4
α-helix	377-410	34
α-helix	422-435	14
α-helix	440-442	3
β-strand	444	1	3
β-strand	446-448	3	4
α-helix	455-463	9
β-strand	473-478	6	3
α-helix	493-498	6
β-strand	502-504	3	3
β-strand	510	1	5
α-helix	514-521	8
β-strand	526-529	4	3
β-strand	532	1	5
α-helix	533-541	9
α-helix	545-548	4
β-strand	550-553	4	3
α-helix	560-576	17
α-helix	579-592	14
α-helix	593-596	4
β-strand	597	1	2
α-helix	598-616	19

Chain C: 26 helices, 22 β-strands

Element	Residues	Length	Sheet
β-strand	28-32	5	11
α-helix	43-58	16
β-strand	62-67	6	11
α-helix	70-76	7
β-strand	77-79	3	11
α-helix	85-96	12
β-strand	101-106	6	11
β-strand	113-117	5	11
α-helix	120-125	6
α-helix	126-137	12
α-helix	146-168	23
β-strand	175-180	6	11
α-helix	181-192	12
β-strand	198-204	7	11
α-helix	208-215	8
α-helix	229-236	8
α-helix	239-251	13
β-strand	254-257	4	11
α-helix	260-269	10
β-strand	276-277	2	11
β-strand	282	1	12
α-helix	293-311	19
α-helix	320-322	3
β-strand	323-329	7	13
α-helix	339-355	17
β-strand	361-367	7	13
β-strand	372-375	4	14
α-helix	377-410	34
α-helix	422-435	14
α-helix	440-442	3
β-strand	444	1	13
β-strand	446-448	3	14
α-helix	455-463	9
β-strand	473-478	6	13
α-helix	493-498	6
β-strand	502-504	3	13
β-strand	510	1	15
α-helix	514-521	8
β-strand	526-529	4	13
β-strand	532	1	15
α-helix	533-541	9
α-helix	545-548	4
β-strand	550-553	4	13
α-helix	560-576	17
α-helix	579-592	14
α-helix	593-596	4
β-strand	597	1	12
α-helix	598-616	19

Chain D: 26 helices, 22 β-strands

Element	Residues	Length	Sheet
β-strand	28-32	5	16
α-helix	43-58	16
β-strand	62-67	6	16
α-helix	70-76	7
β-strand	77-79	3	16
α-helix	85-96	12
β-strand	101-106	6	16
β-strand	113-117	5	16
α-helix	120-125	6
α-helix	126-137	12
α-helix	146-168	23
β-strand	175-180	6	16
α-helix	181-192	12
β-strand	198-204	7	16
α-helix	208-215	8
α-helix	229-236	8
α-helix	239-251	13
β-strand	254-257	4	16
α-helix	260-269	10
β-strand	276-277	2	16
β-strand	282	1	17
α-helix	294-311	18
α-helix	320-322	3
β-strand	323-329	7	18
α-helix	339-355	17
β-strand	361-367	7	18
β-strand	372-375	4	19
α-helix	377-410	34
α-helix	422-435	14
α-helix	440-442	3
β-strand	444	1	18
β-strand	446-448	3	19
α-helix	455-463	9
β-strand	473-478	6	18
α-helix	493-498	6
β-strand	502-504	3	18
β-strand	510	1	20
α-helix	514-521	8
β-strand	526-529	4	18
β-strand	532	1	20
α-helix	533-541	9
α-helix	545-548	4
β-strand	550-553	4	18
α-helix	560-576	17
α-helix	579-592	14
α-helix	593-596	4
β-strand	597	1	17
α-helix	598-616	19

Chains E, F, G and H: 3 helices, 0 β-strands

Element	Residues	Length
α-helix	471-476	6
α-helix	477-479	3
α-helix	489-498	10

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Glycogen [starch] synthase, muscle	A, B, C, D	protein	762	Homo sapiens	P13807 (AlphaFold model)
Glycogenin-2	E, F, G, H	protein	501	Homo sapiens	O15488 (AlphaFold model)

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

>8Z0A_1 Glycogen [starch] synthase, muscle (chains A, B, C, D)
MSYYHHHHHHDYDIPTTENLYFQGAMPLNRTLSMSSLPGLEDWEDEFDLENAVLFEVAWE
VANKVGGIYTVLQTKAKVTGDEWGDNYFLVGPYTEQGVRTQVELLEAPTPALKRTLDSMN
SKGCKVYFGRWLIEGGPLVVLLDVGASAWALERWKGELWDTCNIGVPWYDREANDAVLFG
FLTTWFLGEFLAQSEEKPHVVAHFHEWLAGVGLCLCRARRLPVATIFTTHATLLGRYLCA
GAVDFYNNLENFNVDKEAGERQIYHRYCMERAAAHCAHVFTTVSQITAIEAQHLLKRKPD
IVTPNGLNVKKFSAMHEFQNLHAQSKARIQEFVRGHFYGHLDFNLDKTLYFFIAGRYEFS
NKGADVFLEALARLNYLLRVNGSEQTVVAFFIMPARTNNFNVETLKGQAVRKQLWDTANT
VKEKFGRKLYESLLVGSLPDMNKMLDKEDFTMMKRAIFATQRQSFPPVCTHNMLDDSSDP
ILTTIRRIGLFNSSADRVKVIFHPEFLSSTSPLLPVDYEEFVRGCHLGVFPSYYEPWGYT
PAECTVMGIPSISTNLSGFGCFMEEHIADPSAYGIYILDRRFRSLDDSCSQLTSFLYSFC
QQSRRQRIIQRNRTERLSDLLDWKYLGRYYMSARHMALSKAFPEHFTYEPNEADAAQGYR
YPRPASVPPSPSLSRHSSPHQSEDEEDPRNGPLEEDGERYDEDEEAAKDRRNIRAPEWPR
RASCTSSTSGSKRNSVDTATSSSLSTPSEPLSPTSSLGEERN

Sequence of entity 2 (E, F, G, H), FASTA

>8Z0A_2 Glycogenin-2 (chains E, F, G, H)
MSETEFHHGAQAGLELLRSSNSPTSASQSAGMTVTDQAFVTLATNDIYCQGALVLGQSLR
RHRLTRKLVVLITPQVSSLLRVILSKVFDEVIEVNLIDSADYIHLAFLKRPELGLTLTKL
HCWTLTHYSKCVFLDADTLVLSNVDELFDRGEFSAAPDPGWPDCFNSGVFVFQPSLHTHK
LLLQHAMEHGSFDGADQGLLNSFFRNWSTTDIHKHLPFIYNLSSNTMYTYSPAFKQFGSS
AKVVHFLGSMKPWNYKYNPQSGSVLEQGSASSSQHQAAFLHLWWTVYQNNVLPLYKSVQA
GEARASPGHTLCHSDVGGPCADSASGVGEPCENSTPSAGVPCANSPLGSNQPAQGLPEPT
QIVDETLSLPEGRRSEDMIACPETETPAVITCDPLSQPSPQPADFTETETILPANKVESV
SSEETFEPSQELPAEALRDPSLQDALEVVDLAVSVSQISIEEKVKELSPEEERRKWEEGR
IDYMGKDAFARIQEKLDRFLQ

Primary citation

Human GYS1-GYG2 complex (apo). Chen, P.P., Hsia, K.C. To be published.

Other PDB entries of the same protein (UniProt P13807 (AlphaFold model), which also has an AlphaFold model), best resolution first:

7ZBN 2.62 Å, Cryo-EM structure of the human GS-GN complex in the inhibited state
7Q0B 3.0 Å, Human GYS1-GYG1 complex inhibited state
7Q13 3.0 Å, Human GYS1-GYG1 complex activated state bound to glucose-6-phosphate, uridine…
8CVX 3.5 Å, Human glycogenin-1 and glycogen synthase-1 complex in the presence of glucose-6-phosphate
8CVZ 3.52 Å, Human glycogenin-1 and glycogen synthase-1 complex in the apo ordered state
8CVY 3.6 Å, Human glycogenin-1 and glycogen synthase-1 complex in the apo mobile state
7Q12 3.7 Å, Human GYS1-GYG1 complex activated state bound to glucose-6-phosphate
7Q0S 4.0 Å, Human GYS1-GYG1 complex inhibited-like state bound to glucose-6-phosphate

Browse structure collections

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