8CVY: Glycogen [starch] synthase, muscle

Human glycogenin-1 and glycogen synthase-1 complex in the apo mobile state. Determined by electron microscopy at 3.6 Å resolution. Released 13 Jul 2022.

Method: Electron microscopy
Resolution: 3.6 Å
Organism: Homo sapiens
Chains: 7
Atoms: 17,930
Mol. weight: 409.22 kDa
Released: 13 Jul 2022

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

Secondary structure: helices and β-sheets

8CVY contains 106 α-helices and 74 β-strands across 7 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: 28 helices, 21 β-strands

Element	Residues	Length	Sheet
β-strand	29-32	4	1
α-helix	43-58	16
α-helix	59-61	3
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	125-129	5
α-helix	130-137	8
α-helix	147-168	22
α-helix	171	1
β-strand	176-179	4	1
α-helix	182-184	3
α-helix	185-193	9
β-strand	199-204	6	1
α-helix	208-216	9
α-helix	229-235	7
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	293-311	19
β-strand	324-329	6	3
α-helix	339-355	17
β-strand	362-367	6	3
β-strand	372-375	4	4
α-helix	377-410	34
α-helix	416-419	4
α-helix	422-434	13
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	493-499	7
β-strand	502-504	3	3
α-helix	514-522	9
β-strand	526-527	2	3
β-strand	528-529	2	5
α-helix	533-541	9
β-strand	552-553	2	5
α-helix	560-575	16
α-helix	579-589	11
α-helix	593-596	4
β-strand	597	1	2
α-helix	598-615	18

Chain B: 13 helices, 10 β-strands

Element	Residues	Length	Sheet
α-helix	293-311	19
β-strand	324-329	6	16
α-helix	339-355	17
β-strand	362-367	6	16
β-strand	372-375	4	17
α-helix	377-410	34
α-helix	416-419	4
α-helix	422-434	13
α-helix	440-442	3
β-strand	444	1	16
β-strand	446-448	3	17
α-helix	455-463	9
β-strand	473-477	5	16
α-helix	493-499	7
β-strand	502-504	3	16
α-helix	514-522	9
β-strand	526-527	2	16
β-strand	528-529	2	18
α-helix	533-541	9
β-strand	552-553	2	18
α-helix	560-575	16
α-helix	579-589	11
α-helix	593-596	4

Chain C: 30 helices, 21 β-strands

Element	Residues	Length	Sheet
β-strand	29-32	4	6
α-helix	43-58	16
α-helix	59-61	3
β-strand	62-67	6	6
α-helix	70-76	7
β-strand	77-79	3	6
α-helix	85-96	12
β-strand	102-106	5	6
β-strand	113-117	5	6
α-helix	125-129	5
α-helix	130-136	7
α-helix	146-168	23
α-helix	171	1
β-strand	176-179	4	6
α-helix	182-193	12
β-strand	199-204	6	6
α-helix	208-216	9
α-helix	229-235	7
α-helix	239-251	13
β-strand	254-257	4	6
α-helix	260-269	10
β-strand	276-277	2	6
β-strand	282	1	7
α-helix	284-287	4
α-helix	290-292	3
α-helix	293-311	19
β-strand	324-329	6	8
α-helix	339-355	17
β-strand	362-367	6	8
β-strand	372-375	4	9
α-helix	376	1
α-helix	377-410	34
α-helix	416-419	4
α-helix	422-434	13
α-helix	440-442	3
β-strand	444	1	8
β-strand	446-448	3	9
α-helix	455-463	9
β-strand	473-477	5	8
α-helix	493-499	7
β-strand	502-504	3	8
α-helix	514-522	9
β-strand	526-527	2	8
β-strand	528-529	2	10
α-helix	533-541	9
β-strand	552-553	2	10
α-helix	560-576	17
α-helix	579-591	13
α-helix	593-596	4
β-strand	597	1	7
α-helix	598-615	18

Chain D: 29 helices, 22 β-strands

Element	Residues	Length	Sheet
β-strand	29-32	4	11
α-helix	43-58	16
α-helix	59-61	3
β-strand	62-63	2	11
β-strand	66-67	2	11
α-helix	70-75	6
β-strand	78-79	2	11
α-helix	85-96	12
β-strand	102-105	4	11
β-strand	113-117	5	11
α-helix	120-125	6
α-helix	129-137	9
α-helix	147-168	22
α-helix	171	1
β-strand	176-179	4	11
α-helix	185-193	9
β-strand	199-204	6	11
α-helix	208-216	9
α-helix	229-235	7
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	284-286	3
α-helix	293-311	19
β-strand	324-329	6	13
α-helix	339-355	17
β-strand	362-367	6	13
β-strand	372-375	4	14
α-helix	377-410	34
α-helix	416-419	4
α-helix	422-434	13
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	493-499	7
β-strand	502-504	3	13
α-helix	514-522	9
β-strand	526-527	2	13
β-strand	528-529	2	15
α-helix	533-541	9
β-strand	552-553	2	15
α-helix	560-575	16
α-helix	579-589	11
α-helix	590-592	3
α-helix	593-596	4
β-strand	597	1	12
α-helix	598-615	18

Chain E: 2 helices, 0 β-strands

Element	Residues	Length	Sheet
α-helix	318-327	10
α-helix	338-346	9

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

Element	Residues	Length	Sheet
α-helix	318-327	10
α-helix	338-347	10

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Glycogen [starch] synthase, muscle	A, B, C, D	protein	634	Homo sapiens	P13807 (AlphaFold model)
Glycogenin-1	E, G, H	protein	352	Homo sapiens	P46976 (AlphaFold model)

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

>8CVY_1 Glycogen [starch] synthase, muscle (chains A, B, C, D)
MPLNRTLEMSELPGLEDWEDEFDLENAVLFEVAWEVANKVGGIYTVLQTKAKVTGDEWGD
NYFLVGPYTEQGVRTQVELLEAPTPALKRTLDSMNSKGCKVYFGRWLIEGGPLVVLLDVG
ASAWALERWKGELWDTCNIGVPWYDREANDAVLFGFLTTWFLGEFLAQSEEKPHVVAHFH
EWLAGVGLCLCRARRLPVATIFTTHATLLGRYLCAGAVDFYNNLENFNVDKEAGERQIYH
RYCMERAAAHCAHVFTTVSQITAIEAQHLLKRKPDIVTPNGLNVKKFSAMHEFQNLHAQS
KARIQEFVRGHFYGHLDFNLDKTLYFFIAGRYEFSNKGADVFLEALARLNYLLRVNGSEQ
TVVAFFIMPARTNNFNVETLKGQAVRKQLWDTANTVKEKFGRKLYESLLVGSLPDMNKML
DKEDFTMMKRAIFATQRQSFPPVCTHNMLDDSSDPILTTIRRIGLFNSSADRVKVIFHPE
FLSSTSPLLPVDYEEFVRGCHLGVFPSYYEPWGYTPAECTVMGIPSISTNLSGFGCFMEE
HIADPSAYGIYILDRRFRSLDDSCSQLTSFLYSFCQQSRRQRIIQRNRTERLSDLLDWKY
LGRYYMSARHMALSKAFPEHFTYEPNEADAAQGY

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

>8CVY_2 Glycogenin-1 (chains E, G, H)
GPMTDQAFVTLTTNDAYAKGALVLGSSLKQHRTTRRLVVLATPQVSDSMRKVLETVFDEV
IMVDVLDSGDSAHLTLMKRPELGVTLTKLHCWSLTQYSKCVFMDADTLVLANIDDLFDRE
ELSAAPDPGWPDCFNSGVFVYQPSVETYNQLLHLASEQGSFDGGDQGILNTFFSSWATTD
IRKHLPFIYNLSSISIFSYLPAFKVFGASAKVVHFLGRVKPWNYTYDPKTKSVKSEAHDP
NMTHPEFLILWWNIFTTNVLPLLQQFGLVKDTCSYVNVLSDLVYTLAFSCGFCRKEDVSG
AISHLSLGEIPAMAQPFVSSEERKERWEQGQADYMGADSFDNIKRKLDTYLQ

Primary citation

The structural mechanism of human glycogen synthesis by the GYS1-GYG1 complex. Fastman, N.M., Liu, Y., Ramanan, V. et al. Cell Rep (2022) 40:111041-111041. DOI 10.1016/j.celrep.2022.111041 · 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)
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
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

About this viewer

MolViewer shows 8CVY directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.