5OHT
A GH31 family sulfoquinovosidase from E. coli in complex with aza-sugar inhibitor IFGSQ
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0004553 | molecular_function | hydrolase activity, hydrolyzing O-glycosyl compounds |
| A | 0005975 | biological_process | carbohydrate metabolic process |
| A | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
| A | 0030246 | molecular_function | carbohydrate binding |
| A | 0061720 | biological_process | 6-sulfoquinovose(1-) catabolic process to glycerone phosphate and 3-sulfolactaldehyde |
| A | 1990929 | molecular_function | sulfoquinovosidase activity |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0004553 | molecular_function | hydrolase activity, hydrolyzing O-glycosyl compounds |
| B | 0005975 | biological_process | carbohydrate metabolic process |
| B | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
| B | 0030246 | molecular_function | carbohydrate binding |
| B | 0061720 | biological_process | 6-sulfoquinovose(1-) catabolic process to glycerone phosphate and 3-sulfolactaldehyde |
| B | 1990929 | molecular_function | sulfoquinovosidase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | binding site for residue CA A 701 |
| Chain | Residue |
| A | GLN153 |
| A | GLY154 |
| A | ASP472 |
| A | ASP481 |
| A | HOH928 |
| A | HOH979 |
| site_id | AC2 |
| Number of Residues | 13 |
| Details | binding site for residue 9VH A 702 |
| Chain | Residue |
| A | TRP304 |
| A | MET403 |
| A | ASP405 |
| A | PHE406 |
| A | ARG455 |
| A | ASP472 |
| A | TYR508 |
| A | HIS537 |
| A | HOH865 |
| A | HOH990 |
| A | GLN288 |
| A | ARG301 |
| A | VAL302 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | binding site for residue CA B 701 |
| Chain | Residue |
| B | GLN153 |
| B | GLY154 |
| B | ASP472 |
| B | ASP481 |
| B | HOH879 |
| B | HOH962 |
| site_id | AC4 |
| Number of Residues | 13 |
| Details | binding site for residue 9VH B 702 |
| Chain | Residue |
| B | GLN288 |
| B | ARG301 |
| B | VAL302 |
| B | TRP304 |
| B | MET403 |
| B | ASP405 |
| B | PHE406 |
| B | ARG455 |
| B | ASP472 |
| B | TYR508 |
| B | HIS537 |
| B | HOH814 |
| B | HOH848 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | ACT_SITE: Nucleophile => ECO:0000269|PubMed:26878550 |
| Chain | Residue | Details |
| A | ASP405 | |
| B | ASP405 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | ACT_SITE: ACT_SITE => ECO:0000250|UniProtKB:P31434 |
| Chain | Residue | Details |
| A | GLU408 | |
| B | GLU408 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | ACT_SITE: Proton donor => ECO:0000305|PubMed:26878550 |
| Chain | Residue | Details |
| A | ASP472 | |
| B | ASP472 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 10 |
| Details | BINDING: BINDING => ECO:0000305|PubMed:26878550, ECO:0007744|PDB:5AEE |
| Chain | Residue | Details |
| A | GLN288 | |
| B | HIS537 | |
| A | ARG301 | |
| A | VAL302 | |
| A | TRP304 | |
| A | HIS537 | |
| B | GLN288 | |
| B | ARG301 | |
| B | VAL302 | |
| B | TRP304 |
