Research workbench
Human GYS1-GYG1 complex activated state bound to glucose-6-phosphate
Analyse Human GYS1-GYG1 complex activated state bound to glucose-6-phosphate in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7Q12
- Type
- protein
- Length
- 2,488 residues
- Chains
- 8
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P13807, P46976
- Ligands
- G6P
Structure
electron microscopy · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | — | protein | 590 | — | P13807 |
| E, F, G, H | — | protein | 32 | — | P46976 |
Ligands and binding sites
- G6P · 6-O-phosphono-alpha-D-glucopyranose · sugar · 4 copies · chains A, C, B, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 7Q12 · Human GYS1-GYG1 complex activated state bound to glucose-6-phosphate · the same entry in another collection · chain D against D, TM-score 1.00
- P13807 · AlphaFold monomer V2.0 prediction for glycogen [starch] synthase, muscle (P13807) · a predicted model of the same protein · chain A against A, TM-score 0.95
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 7Q12 · PDBe 7Q12 · UniProt P13807 · UniProt P46976
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