7ZBN: Human GS-GN complex in the inhibited state

Cryo-EM structure of the human GS-GN complex in the inhibited state. Determined by electron microscopy at 2.62 Å resolution. Released 22 Jun 2022.

Method: Electron microscopy
Resolution: 2.62 Å
Organism: Homo sapiens
Chains: 8
Atoms: 21,122
Mol. weight: 485.58 kDa
Released: 22 Jun 2022

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

Secondary structure: helices and β-sheets

7ZBN contains 116 α-helices and 96 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 C: 27 helices, 24 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	70-75	6
β-strand	77-79	3	1
α-helix	85-96	12
β-strand	100-106	7	1
β-strand	113-118	6	1
α-helix	120-125	6
α-helix	126-137	12
α-helix	146-167	22
β-strand	175-179	5	1
α-helix	182-194	13
β-strand	198-204	7	1
α-helix	208-216	9
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	284-286	3
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	416-419	4
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	473-477	5	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
β-strand	542	1	6
α-helix	545-548	4
β-strand	550-553	4	3
α-helix	560-576	17
α-helix	579-591	13
α-helix	592-596	5
β-strand	597	1	2
α-helix	598-616	19
β-strand	636	1	6

Chain B: 27 helices, 24 β-strands

Element	Residues	Length	Sheet
β-strand	28-32	5	7
α-helix	43-58	16
β-strand	62-67	6	7
α-helix	70-75	6
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	120-125	6
α-helix	126-137	12
α-helix	146-167	22
β-strand	175-179	5	7
α-helix	182-194	13
β-strand	198-204	7	7
α-helix	208-216	9
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	284-286	3
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	416-419	4
α-helix	422-435	14
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	493-498	6
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
β-strand	542	1	12
α-helix	545-548	4
β-strand	550-553	4	9
α-helix	560-575	16
α-helix	579-591	13
α-helix	592-596	5
β-strand	597	1	8
α-helix	598-616	19
β-strand	636	1	12

Chain D: 27 helices, 24 β-strands

Element	Residues	Length	Sheet
β-strand	28-32	5	19
α-helix	43-58	16
β-strand	62-67	6	19
α-helix	70-75	6
β-strand	77-79	3	19
α-helix	85-96	12
β-strand	101-106	6	19
β-strand	113-117	5	19
α-helix	120-125	6
α-helix	126-137	12
α-helix	146-167	22
β-strand	175-179	5	19
α-helix	182-194	13
β-strand	198-204	7	19
α-helix	208-216	9
α-helix	229-235	7
α-helix	239-250	12
β-strand	254-257	4	19
α-helix	260-269	10
β-strand	276-277	2	19
β-strand	282	1	20
α-helix	284-286	3
α-helix	294-311	18
β-strand	323-329	7	21
α-helix	339-355	17
β-strand	361-367	7	21
β-strand	372-375	4	22
α-helix	377-409	33
α-helix	416-419	4
α-helix	422-435	14
α-helix	440-442	3
β-strand	444	1	21
β-strand	446-448	3	22
α-helix	455-463	9
β-strand	473-477	5	21
α-helix	493-498	6
β-strand	502-504	3	21
β-strand	510	1	23
α-helix	514-521	8
β-strand	526-529	4	21
β-strand	532	1	23
α-helix	533-541	9
β-strand	542	1	24
α-helix	545-548	4
β-strand	550-553	4	21
α-helix	560-576	17
α-helix	579-591	13
α-helix	592-596	5
β-strand	597	1	20
α-helix	598-616	19
β-strand	636	1	24

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

Element	Residues	Length	Sheet
α-helix	302-310	9
α-helix	321-330	10

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

Element	Residues	Length	Sheet
α-helix	302-310	9
α-helix	321-329	9

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Glycogen [starch] synthase, muscle	A, C	protein	737	Homo sapiens	P13807 (AlphaFold model)
Glycogen [starch] synthase, muscle	B, D	protein	737	Homo sapiens	P13807 (AlphaFold model)
Isoform GN-1 of Glycogenin-1	E, F, G, H	protein	333	Homo sapiens	P46976 (AlphaFold model)

Sequence of entity 1 (A, C), FASTA

>7ZBN_1 Glycogen [starch] synthase, muscle (chains A, C)
MPLNRTLSMSSLPGLEDWEDEFDLENAVLFEVAWEVANKVGGIYTVLQTKAKVTGDEWGD
NYFLVGPYTEQGVRTQVELLEAPTPALKRTLDSMNSKGCKVYFGRWLIEGGPLVVLLDVG
ASAWALERWKGELWDTCNIGVPWYDREANDAVLFGFLTTWFLGEFLAQSEEKPHVVAHFH
EWLAGVGLCLCRARRLPVATIFTTHATLLGRYLCAGAVDFYNNLENFNVDKEAGERQIYH
RYCMERAAAHCAHVFTTVSQITAIEAQHLLKRKPDIVTPNGLNVKKFSAMHEFQNLHAQS
KARIQEFVRGHFYGHLDFNLDKTLYFFIAGRYEFSNKGADVFLEALARLNYLLRVNGSEQ
TVVAFFIMPARTNNFNVETLKGQAVRKQLWDTANTVKEKFGRKLYESLLVGSLPDMNKML
DKEDFTMMKRAIFATQRQSFPPVCTHNMLDDSSDPILTTIRRIGLFNSSADRVKVIFHPE
FLSSTSPLLPVDYEEFVRGCHLGVFPSYYEPWGYTPAECTVMGIPSISTNLSGFGCFMEE
HIADPSAYGIYILDRRFRSLDDSCSQLTSFLYSFCQQSRRQRIIQRNRTERLSDLLDWKY
LGRYYMSARHMALSKAFPEHFTYEPNEADAAQGYRYPRPASVPPSPSLSRHSSPHQSEDE
EDPRNGPLEEDGERYDEDEEAAKDRRNIRAPEWPRRASCTSSTSGSKRNSVDTATSSSLS
TPSEPLSPTSSLGEERN

Sequence of entity 2 (B, D), FASTA

>7ZBN_2 Glycogen [starch] synthase, muscle (chains B, D)
MPLNRTLSMSSLPGLEDWEDEFDLENAVLFEVAWEVANKVGGIYTVLQTKAKVTGDEWGD
NYFLVGPYTEQGVRTQVELLEAPTPALKRTLDSMNSKGCKVYFGRWLIEGGPLVVLLDVG
ASAWALERWKGELWDTCNIGVPWYDREANDAVLFGFLTTWFLGEFLAQSEEKPHVVAHFH
EWLAGVGLCLCRARRLPVATIFTTHATLLGRYLCAGAVDFYNNLENFNVDKEAGERQIYH
RYCMERAAAHCAHVFTTVSQITAIEAQHLLKRKPDIVTPNGLNVKKFSAMHEFQNLHAQS
KARIQEFVRGHFYGHLDFNLDKTLYFFIAGRYEFSNKGADVFLEALARLNYLLRVNGSEQ
TVVAFFIMPARTNNFNVETLKGQAVRKQLWDTANTVKEKFGRKLYESLLVGSLPDMNKML
DKEDFTMMKRAIFATQRQSFPPVCTHNMLDDSSDPILTTIRRIGLFNSSADRVKVIFHPE
FLSSTSPLLPVDYEEFVRGCHLGVFPSYYEPWGYTPAECTVMGIPSISTNLSGFGCFMEE
HIADPSAYGIYILDRRFRSLDDSCSQLTSFLYSFCQQSRRQRIIQRNRTERLSDLLDWKY
LGRYYMSARHMALSKAFPEHFTYEPNEADAAQGYRYPRPASVPPSPSLSRHSSPHQSEDE
EDPRNGPLEEDGERYDEDEEAAKDRRNIRAPEWPRRASCTSSTSGSKRNSVDTATSSSLS
TPSEPLSPTSSLGEERN

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

>7ZBN_3 Isoform GN-1 of Glycogenin-1 (chains E, F, G, H)
MADQAFVTLTTNDAYAKGALVLGSSLKQHRTTRRLVVLATPQVSDSMRKVLETVFDEVIM
VDVLDSGDSAHLTLMKRPELGVTLTKLHCWSLTQYSKCVFMDADTLVLANIDDLFDREEL
SAAPDPGWPDCFNSGVFVYQPSVETYNQLLHLASEQGSFDGGDQGILNTFFSSWATTDIR
KHLPFIYNLSSISIFSYLPAFKVFGASAKVVHFLGRVKPWNYTYDPKTKSVKSEAHDPNM
THPEFLILWWNIFTTNVLPLLQQFGLVKDTCSYVNVEDVSGAISHLSLGEIPAMAQPFVS
SEERKERWEQGQADYMGADSFDNIKRKLDTYLQ

Primary citation

Mechanism of glycogen synthase inactivation and interaction with glycogenin. Marr, L., Biswas, D., Daly, L.A. et al. Nat Commun (2022) 13:3372-3372. DOI 10.1038/s41467-022-31109-6 · PubMed

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

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

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