7VL5
The complex structure of beta-1,2-glucosyltransferase from Ignavibacterium album with n-octyl-beta-D-glucoside
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004553 | molecular_function | hydrolase activity, hydrolyzing O-glycosyl compounds |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005975 | biological_process | carbohydrate metabolic process |
| A | 0016740 | molecular_function | transferase activity |
| A | 0016757 | molecular_function | glycosyltransferase activity |
| B | 0004553 | molecular_function | hydrolase activity, hydrolyzing O-glycosyl compounds |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005975 | biological_process | carbohydrate metabolic process |
| B | 0016740 | molecular_function | transferase activity |
| B | 0016757 | molecular_function | glycosyltransferase activity |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | ACT_SITE: Proton donor/acceptor => ECO:0000305|PubMed:35065074 |
| Chain | Residue | Details |
| A | GLU176 | |
| B | GLU176 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | ACT_SITE: Nucleophile => ECO:0000305|PubMed:35065074 |
| Chain | Residue | Details |
| A | GLU343 | |
| B | GLU343 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 22 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:35065074, ECO:0007744|PDB:7VKY |
| Chain | Residue | Details |
| A | TYR52 | |
| A | ARG349 | |
| A | TYR378 | |
| B | TYR52 | |
| B | ILE99 | |
| B | ALA101 | |
| B | GLU102 | |
| B | ASN175 | |
| B | GLU176 | |
| B | GLY278 | |
| B | TRP279 | |
| A | ILE99 | |
| B | GLU343 | |
| B | ARG349 | |
| B | TYR378 | |
| A | ALA101 | |
| A | GLU102 | |
| A | ASN175 | |
| A | GLU176 | |
| A | GLY278 | |
| A | TRP279 | |
| A | GLU343 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 8 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:35065074, ECO:0007744|PDB:7VKX |
| Chain | Residue | Details |
| A | LYS358 | |
| A | GLU361 | |
| A | SER708 | |
| A | TYR709 | |
| B | LYS358 | |
| B | GLU361 | |
| B | SER708 | |
| B | TYR709 |
