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Inhibited state structure of YGSY2P
Analyse Inhibited state structure of YGSY2P in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5SUL
- Type
- protein
- Length
- 1,225 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Glycogen [starch] synthase isoform 2
- EC
- 2.4.1.11
- UniProt
- P27472
- Ligands
- UDP, U5P
- Pockets
- 10 · best druggability 0.71
Structure
x-ray diffraction · 2 distinct chains · 49% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Glycogen [starch] synthase isoform 2 (EC 2.4.1.11) | protein | 619 | 48% helix, 15% strand | P27472 |
| B | Glycogen [starch] synthase isoform 2 (EC 2.4.1.11) | protein | 606 | 50% helix, 15% strand | P27472 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
10 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 825 | 0.71 | 0.76 | 72 | U5P |
| 2 | 593 | 0.68 | 0.77 | 53 | UDP |
| 3 | 623 | 0.65 | 0.76 | 65 | empty |
| 4 | 131 | 0.41 | 0.75 | 25 | empty |
| 5 | 103 | 0.39 | 0.76 | 21 | empty |
Interfaces
1 interface between chains.
- A–B · 239 Ų buried · 6 hydrogen bonds · protein-protein
Compared structures
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 P27472
- Elsewhere: RCSB PDB 5SUL · PDBe 5SUL · UniProt P27472
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