7Q0B: Human GYS1-GYG1 complex inhibited state

Human GYS1-GYG1 complex inhibited state. Determined by electron microscopy at 3.0 Å resolution. Released 27 Jul 2022.

Method: Electron microscopy
Resolution: 3.0 Å
Organism: Homo sapiens
Chains: 8
Atoms: 21,168
Mol. weight: 493.39 kDa
Released: 27 Jul 2022

Explore 7Q0B in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

7Q0B contains 127 α-helices and 92 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: 29 helices, 24 β-strands

Element	Residues	Length	Sheet
β-strand	27-32	6	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	119-121	3
α-helix	123-125	3
α-helix	126-137	12
α-helix	148-167	20
β-strand	174-179	6	1
α-helix	182-184	3
α-helix	185-193	9
β-strand	198-204	7	1
α-helix	208-214	7
α-helix	229-235	7
α-helix	239-250	12
β-strand	254-257	4	1
α-helix	260-269	10
β-strand	276-277	2	1
β-strand	282	1	2
α-helix	284-287	4
α-helix	294-311	18
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	377-409	33
α-helix	422-434	13
β-strand	444	1	3
β-strand	446-448	3	4
α-helix	455-463	9
β-strand	473-477	5	3
α-helix	481-482	2
α-helix	493-497	5
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
β-strand	542	1	6
α-helix	545-548	4
β-strand	550-553	4	3
α-helix	560-575	16
α-helix	579-590	12
α-helix	593-596	4
β-strand	597	1	2
α-helix	598-601	4
α-helix	603-616	14
β-strand	638	1	6

Chains B and C: 30 helices, 22 β-strands

Element	Residues	Length	Sheet
β-strand	27-32	6	7
α-helix	43-58	16
β-strand	62-67	6	7
α-helix	70-76	7
β-strand	77-79	3	7
α-helix	85-96	12
β-strand	101-106	6	7
β-strand	113-117	5	7
α-helix	119-121	3
α-helix	123-125	3
α-helix	126-137	12
α-helix	148-167	20
β-strand	174-179	6	7
α-helix	182-184	3
α-helix	185-193	9
β-strand	198-204	7	7
α-helix	208-214	7
α-helix	229-235	7
α-helix	239-250	12
β-strand	254-257	4	7
α-helix	260-269	10
β-strand	276-277	2	7
β-strand	282	1	8
α-helix	284-287	4
α-helix	294-311	18
β-strand	323-329	7	9
α-helix	339-355	17
β-strand	361-367	7	9
β-strand	372-375	4	10
α-helix	377-409	33
α-helix	422-434	13
α-helix	440-442	3
β-strand	444	1	9
β-strand	446-448	3	10
α-helix	455-463	9
β-strand	473-477	5	9
α-helix	481-482	2
α-helix	493-497	5
β-strand	502-504	3	9
β-strand	510	1	11
α-helix	514-521	8
β-strand	526-529	4	9
β-strand	532	1	11
α-helix	533-541	9
α-helix	545-548	4
β-strand	550-553	4	9
α-helix	560-575	16
α-helix	579-590	12
α-helix	593-596	4
β-strand	597	1	8
α-helix	598-601	4
α-helix	603-616	14

Chain D: 30 helices, 24 β-strands

Element	Residues	Length	Sheet
β-strand	27-32	6	17
α-helix	43-58	16
β-strand	62-67	6	17
α-helix	70-76	7
β-strand	77-79	3	17
α-helix	85-96	12
β-strand	101-106	6	17
β-strand	113-117	5	17
α-helix	119-121	3
α-helix	123-125	3
α-helix	126-137	12
α-helix	148-167	20
β-strand	174-179	6	17
α-helix	182-184	3
α-helix	185-193	9
β-strand	198-204	7	17
α-helix	208-214	7
α-helix	229-235	7
α-helix	239-250	12
β-strand	254-257	4	17
α-helix	260-269	10
β-strand	276-277	2	17
β-strand	282	1	18
α-helix	284-287	4
α-helix	294-311	18
β-strand	323-329	7	19
α-helix	339-355	17
β-strand	361-367	7	19
β-strand	372-375	4	20
α-helix	377-409	33
α-helix	422-434	13
α-helix	440-442	3
β-strand	444	1	19
β-strand	446-448	3	20
α-helix	455-463	9
β-strand	473-477	5	19
α-helix	481-482	2
α-helix	493-497	5
β-strand	502-504	3	19
β-strand	510	1	21
α-helix	514-521	8
β-strand	526-529	4	19
β-strand	532	1	21
α-helix	533-541	9
β-strand	542	1	22
α-helix	545-548	4
β-strand	550-553	4	19
α-helix	560-575	16
α-helix	579-590	12
α-helix	593-596	4
β-strand	597	1	18
α-helix	598-601	4
α-helix	603-616	14
β-strand	638	1	22

Chains E, F, G and H: 2 helices, 0 β-strands

Element	Residues	Length	Sheet
α-helix	319-327	9
α-helix	338-345	8

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Glycogen [starch] synthase, muscle	A, D	protein	737	Homo sapiens	P13807 (AlphaFold model)
Glycogen [starch] synthase, muscle	B, C	protein	737	Homo sapiens	P13807 (AlphaFold model)
Glycogenin-1	E, F, G, H	protein	350	Homo sapiens	P46976 (AlphaFold model)

Sequence of entity 1 (A, D), FASTA

>7Q0B_1 Glycogen [starch] synthase, muscle (chains A, D)
MPLNRTLSMSSLPGLEDWEDEFDLENAVLFEVAWEVANKVGGIYTVLQTKAKVTGDEWGD
NYFLVGPYTEQGVRTQVELLEAPTPALKRTLDSMNSKGCKVYFGRWLIEGGPLVVLLDVG
ASAWALERWKGELWDTCNIGVPWYDREANDAVLFGFLTTWFLGEFLAQSEEKPHVVAHFH
EWLAGVGLCLCRARRLPVATIFTTHATLLGRYLCAGAVDFYNNLENFNVDKEAGERQIYH
RYCMERAAAHCAHVFTTVSQITAIEAQHLLKRKPDIVTPNGLNVKKFSAMHEFQNLHAQS
KARIQEFVRGHFYGHLDFNLDKTLYFFIAGRYEFSNKGADVFLEALARLNYLLRVNGSEQ
TVVAFFIMPARTNNFNVETLKGQAVRKQLWDTANTVKEKFGRKLYESLLVGSLPDMNKML
DKEDFTMMKRAIFATQRQSFPPVCTHNMLDDSSDPILTTIRRIGLFNSSADRVKVIFHPE
FLSSTSPLLPVDYEEFVRGCHLGVFPSYYEPWGYTPAECTVMGIPSISTNLSGFGCFMEE
HIADPSAYGIYILDRRFRSLDDSCSQLTSFLYSFCQQSRRQRIIQRNRTERLSDLLDWKY
LGRYYMSARHMALSKAFPEHFTYEPNEADAAQGYRYPRPASVPPSPSLSRHSSPHQSEDE
EDPRNGPLEEDGERYDEDEEAAKDRRNIRAPEWPRRASCTSSTSGSKRNSVDTATSSSLS
TPSEPLSPTSSLGEERN

Sequence of entity 2 (B, C), FASTA

>7Q0B_2 Glycogen [starch] synthase, muscle (chains B, C)
MPLNRTLSMSSLPGLEDWEDEFDLENAVLFEVAWEVANKVGGIYTVLQTKAKVTGDEWGD
NYFLVGPYTEQGVRTQVELLEAPTPALKRTLDSMNSKGCKVYFGRWLIEGGPLVVLLDVG
ASAWALERWKGELWDTCNIGVPWYDREANDAVLFGFLTTWFLGEFLAQSEEKPHVVAHFH
EWLAGVGLCLCRARRLPVATIFTTHATLLGRYLCAGAVDFYNNLENFNVDKEAGERQIYH
RYCMERAAAHCAHVFTTVSQITAIEAQHLLKRKPDIVTPNGLNVKKFSAMHEFQNLHAQS
KARIQEFVRGHFYGHLDFNLDKTLYFFIAGRYEFSNKGADVFLEALARLNYLLRVNGSEQ
TVVAFFIMPARTNNFNVETLKGQAVRKQLWDTANTVKEKFGRKLYESLLVGSLPDMNKML
DKEDFTMMKRAIFATQRQSFPPVCTHNMLDDSSDPILTTIRRIGLFNSSADRVKVIFHPE
FLSSTSPLLPVDYEEFVRGCHLGVFPSYYEPWGYTPAECTVMGIPSISTNLSGFGCFMEE
HIADPSAYGIYILDRRFRSLDDSCSQLTSFLYSFCQQSRRQRIIQRNRTERLSDLLDWKY
LGRYYMSARHMALSKAFPEHFTYEPNEADAAQGYRYPRPASVPPSPSLSRHSSPHQSEDE
EDPRNGPLEEDGERYDEDEEAAKDRRNIRAPEWPRRASCTSSTSGSKRNSVDTATSSSLS
TPSEPLSPTSSLGEERN

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

>7Q0B_3 Glycogenin-1 (chains E, F, G, H)
MTDQAFVTLTTNDAYAKGALVLGSSLKQHRTTRRLVVLATPQVSDSMRKVLETVFDEVIM
VDVLDSGDSAHLTLMKRPELGVTLTKLHCWSLTQYSKCVFMDADTLVLANIDDLFDREEL
SAAPDPGWPDCFNSGVFVYQPSVETYNQLLHLASEQGSFDGGDQGILNTFFSSWATTDIR
KHLPFIYNLSSISIYSYLPAFKVFGASAKVVHFLGRVKPWNYTYDPKTKSVKSEAHDPNM
THPEFLILWWNIFTTNVLPLLQQFGLVKDTCSYVNVLSDLVYTLAFSCGFCRKEDVSGAI
SHLSLGEIPAMAQPFVSSEERKERWEQGQADYMGADSFDNIKRKLDTYLQ

Primary citation

Molecular basis for the regulation of human glycogen synthase by phosphorylation and glucose-6-phosphate. McCorvie, T.J., Loria, P.M., Tu, M. et al. Nat Struct Mol Biol (2022) 29:628-638. DOI 10.1038/s41594-022-00799-3 · PubMed

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
8Z0A 2.84 Å, Human GYS1-GYG2 complex (apo)
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

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