Research workbench

Human GYS1-GYG1 complex inhibited state

Analyse Human GYS1-GYG1 complex inhibited state in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7Q0B
Type: protein
Length: 2,618 residues
Chains: 8
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Glycogen [starch] synthase, muscle; Glycogenin-1
EC: 2.4.1.11, 2.4.1.186
UniProt: P13807, P46976
Pockets: 20 · best druggability 0.76

Structure

electron microscopy · 3 distinct chains · 47% helix, 14% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, D	Glycogen [starch] synthase, muscle (EC 2.4.1.11)	protein	620	47% helix, 14% strand	P13807
B, C	Glycogen [starch] synthase, muscle (EC 2.4.1.11)	protein	623	47% helix, 14% strand	P13807
E, F, G, H	Glycogenin-1 (EC 2.4.1.186)	protein	33	52% helix, 0% strand	P46976

Pockets

20 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1009	0.76	0.79	103	empty
2	1057	0.76	0.78	105	empty
3	646	0.69	0.77	68	empty
4	693	0.69	0.76	66	empty
5	589	0.68	0.77	58	empty

Interfaces

10 interfaces between chains.

B–C · 1444 Å² buried · 4 hydrogen bonds · protein-protein
A–D · 1436 Å² buried · 4 hydrogen bonds · protein-protein
C–G · 1212 Å² buried · 6 hydrogen bonds · protein-protein
D–H · 1208 Å² buried · 6 hydrogen bonds · protein-protein
A–E · 1204 Å² buried · 8 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 modified (phosphorylation).

Compared structures

7Q0B · Human GYS1-GYG1 complex inhibited state · the same entry in another collection · chain H against H, TM-score 1.00
P13807 · AlphaFold monomer V2.0 prediction for glycogen [starch] synthase, muscle (P13807) · a predicted model of the same protein · chain C against A, TM-score 0.97

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt P13807
Every structure of UniProt P46976
Elsewhere: RCSB PDB 7Q0B · PDBe 7Q0B · UniProt P13807 · UniProt P46976

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