8CVX: Glycogen [starch] synthase, muscle

Human glycogenin-1 and glycogen synthase-1 complex in the presence of glucose-6-phosphate. Determined by electron microscopy at 3.5 Å resolution. Released 13 Jul 2022.

Method: Electron microscopy
Resolution: 3.5 Å
Organism: Homo sapiens
Chains: 8
Atoms: 20,448
Mol. weight: 449.82 kDa
Ligands: G6P
Released: 13 Jul 2022

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

Secondary structure: helices and β-sheets

8CVX contains 111 α-helices and 93 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: 27 helices, 23 β-strands

Element	Residues	Length	Sheet
β-strand	30-33	4	1
α-helix	43-57	15
β-strand	63-67	5	1
α-helix	70-76	7
β-strand	77-79	3	1
α-helix	85-95	11
β-strand	101-106	6	1
β-strand	113-117	5	1
α-helix	119-121	3
α-helix	122-136	15
α-helix	146-168	23
α-helix	172-174	3
β-strand	175-180	6	1
α-helix	182-184	3
α-helix	186-193	8
β-strand	198-204	7	1
α-helix	208-216	9
α-helix	231-235	5
α-helix	239-248	10
β-strand	254-257	4	1
α-helix	260-265	6
α-helix	266-270	5
β-strand	276-277	2	1
β-strand	282	1	2
α-helix	292-311	20
β-strand	323-329	7	3
α-helix	339-352	14
β-strand	361-367	7	3
β-strand	372-375	4	4
α-helix	377-408	32
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
β-strand	483	1	5
β-strand	490	1	5
α-helix	493-499	7
β-strand	502-504	3	3
α-helix	514-521	8
β-strand	526-527	2	3
β-strand	528-529	2	6
α-helix	533-540	8
β-strand	552-553	2	6
α-helix	560-575	16
α-helix	579-590	12
β-strand	597	1	2
α-helix	598-601	4
α-helix	603-616	14

Chain B: 24 helices, 24 β-strands

Element	Residues	Length	Sheet
β-strand	29-32	4	7
α-helix	43-57	15
β-strand	63-67	5	7
α-helix	70-76	7
β-strand	77-79	3	7
α-helix	85-95	11
α-helix	96-98	3
β-strand	101	1	7
β-strand	104-106	3	7
β-strand	113-117	5	7
α-helix	126-136	11
α-helix	146-168	23
α-helix	172-174	3
β-strand	175-180	6	7
α-helix	182-193	12
β-strand	198-204	7	7
α-helix	208-216	9
α-helix	231-235	5
α-helix	239-248	10
β-strand	254-257	4	7
α-helix	260-266	7
β-strand	276-277	2	7
β-strand	282	1	8
α-helix	292-311	20
β-strand	323-329	7	9
α-helix	339-352	14
β-strand	361-367	7	9
β-strand	372-375	4	10
α-helix	377-408	32
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
β-strand	483	1	11
β-strand	490	1	11
α-helix	493-499	7
β-strand	502-504	3	9
α-helix	515-521	7
β-strand	526-527	2	9
β-strand	528-529	2	12
α-helix	533-540	8
β-strand	552-553	2	12
α-helix	560-575	16
α-helix	579-590	12
β-strand	597	1	8
α-helix	598-616	19

Chain C: 25 helices, 23 β-strands

Element	Residues	Length	Sheet
β-strand	27-33	7	19
α-helix	43-57	15
β-strand	63-68	6	19
α-helix	70-76	7
β-strand	77-79	3	19
α-helix	85-96	12
β-strand	101-106	6	19
β-strand	113-118	6	19
α-helix	125-134	10
α-helix	146-168	23
α-helix	172-173	2
β-strand	174-180	7	19
α-helix	182-193	12
β-strand	198-204	7	19
α-helix	208-216	9
α-helix	231-235	5
α-helix	239-248	10
β-strand	254-257	4	19
α-helix	260-268	9
β-strand	276-277	2	19
β-strand	282	1	20
α-helix	284-287	4
α-helix	292-311	20
β-strand	323-329	7	21
α-helix	339-352	14
β-strand	361-367	7	21
β-strand	372-375	4	22
α-helix	377-408	32
α-helix	422-434	13
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
β-strand	483	1	23
β-strand	490	1	23
α-helix	493-499	7
β-strand	502-504	3	21
α-helix	515-521	7
β-strand	526-527	2	21
β-strand	528-529	2	24
α-helix	533-540	8
β-strand	552-553	2	24
α-helix	560-575	16
α-helix	579-590	12
β-strand	597	1	20
α-helix	598-601	4
α-helix	603-616	14

Chain D: 24 helices, 23 β-strands

Element	Residues	Length	Sheet
β-strand	29-33	5	13
α-helix	43-57	15
β-strand	63-68	6	13
α-helix	70-76	7
β-strand	77-79	3	13
α-helix	85-95	11
α-helix	96-98	3
β-strand	101	1	13
β-strand	104-106	3	13
β-strand	113-118	6	13
α-helix	126-134	9
α-helix	146-168	23
α-helix	172-174	3
β-strand	175-180	6	13
α-helix	182-194	13
β-strand	198-204	7	13
α-helix	208-216	9
α-helix	231-235	5
α-helix	239-249	11
β-strand	254-257	4	13
α-helix	260-268	9
β-strand	276-277	2	13
β-strand	282	1	14
α-helix	292-311	20
β-strand	323-329	7	15
α-helix	339-352	14
β-strand	361-367	7	15
β-strand	374-375	2	16
α-helix	377-408	32
α-helix	422-435	14
α-helix	440-442	3
β-strand	444	1	17
β-strand	446-447	2	16
α-helix	455-463	9
β-strand	473-475	3	15
β-strand	477	1	17
α-helix	493-499	7
β-strand	502-504	3	15
α-helix	515-521	7
β-strand	526-527	2	15
β-strand	528-529	2	18
α-helix	533-540	8
β-strand	552-553	2	18
α-helix	560-575	16
α-helix	579-590	12
β-strand	597	1	14
α-helix	598-616	19

Chain E: 2 helices, 0 β-strands

Element	Residues	Length	Sheet
α-helix	319-325	7
α-helix	338-349	12

Chain F: 3 helices, 0 β-strands

Element	Residues	Length
α-helix	321-325	5
α-helix	326-328	3
α-helix	338-345	8

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

Element	Residues	Length
α-helix	320-325	6
α-helix	326-328	3
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, F, G, H	protein	352	Homo sapiens	P46976 (AlphaFold model)

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

>8CVX_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, F, G, H), FASTA

>8CVX_2 Glycogenin-1 (chains E, F, G, H)
GPMTDQAFVTLTTNDAYAKGALVLGSSLKQHRTTRRLVVLATPQVSDSMRKVLETVFDEV
IMVDVLDSGDSAHLTLMKRPELGVTLTKLHCWSLTQYSKCVFMDADTLVLANIDDLFDRE
ELSAAPDPGWPDCFNSGVFVYQPSVETYNQLLHLASEQGSFDGGDQGILNTFFSSWATTD
IRKHLPFIYNLSSISIFSYLPAFKVFGASAKVVHFLGRVKPWNYTYDPKTKSVKSEAHDP
NMTHPEFLILWWNIFTTNVLPLLQQFGLVKDTCSYVNVLSDLVYTLAFSCGFCRKEDVSG
AISHLSLGEIPAMAQPFVSSEERKERWEQGQADYMGADSFDNIKRKLDTYLQ

Ligands and cofactors

ID	Name	Formula	Copies
G6P	6-O-phosphono-alpha-D-glucopyranose	C6 H13 O9 P	4

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…
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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