Research workbench
A GH31 family sulfoquinovosidase from E. rectale in complex with aza- sugar inhibitor ifgsq
Analyse A GH31 family sulfoquinovosidase from E. rectale in complex with aza- sugar… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6PNR
- Type
- protein
- Length
- 1,334 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Alpha-glucosidase
- EC
- 3.2.1.20
- UniProt
- A0A396FTG2
- Ligands
- 9VH, SO4
- Pockets
- 9 · best druggability 0.78
Structure
x-ray diffraction · 1 distinct chain · 28% helix, 29% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C | Alpha-glucosidase (EC 3.2.1.20) | protein | 667 | 28% helix, 29% strand | A0A396FTG2 |
Ligands and binding sites
- 9VH · [(3~{S},4~{R},5~{R})-4,5-bis(oxidanyl)piperidin-3-yl]methanesulfonic acid · ligand · 2 copies · chains A, C
- SO4 · Sulfate ion · ion · 13 copies · chains A, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
9 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 249 | 0.78 | 0.91 | 35 | 9VH |
| 2 | 1009 | 0.77 | 0.79 | 89 | empty |
| 3 | 237 | 0.76 | 0.90 | 37 | 9VH |
| 4 | 336 | 0.55 | 0.75 | 52 | empty |
| 5 | 131 | 0.49 | 0.79 | 29 | empty |
Interfaces
1 interface between chains.
- A–C · 704 Ų buried · 13 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 disulfide (disulfide).
Compared structures
- 6PNR · A GH31 family sulfoquinovosidase from E. rectale in complex with aza-sugar inhibitor IFGSQ · 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 A0A396FTG2
- Elsewhere: RCSB PDB 6PNR · PDBe 6PNR · UniProt A0A396FTG2
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.