Research workbench
Structure of the C domain of glycogen synthase from pyrococcus abyssi
Analyse Structure of the C domain of glycogen synthase from pyrococcus abyssi in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2BFW
- Type
- protein
- Length
- 196 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Glga glycogen synthase
- EC
- 2.4.1.21
- UniProt
- Q9V2J8
- Ligands
- SO4
- Pockets
- 1 · best druggability 0.44
Structure
x-ray diffraction · 1 distinct chain · 48% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Glga glycogen synthase (EC 2.4.1.21) | protein | 196 | 48% helix, 15% strand | Q9V2J8 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 151 | 0.44 | 0.75 | 26 | SO4, ACT |
Compared structures
- 2BFW · Structure of the C domain of glycogen synthase from Pyrococcus abyssi · the same entry in another collection · chain A against A, TM-score 1.00
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 Q9V2J8
- Elsewhere: RCSB PDB 2BFW · PDBe 2BFW · UniProt Q9V2J8
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