5AED
A bacterial protein structure in glycoside hydrolase family 31
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 | 4 |
| Details | BINDING SITE FOR RESIDUE MPD A 1682 |
| Chain | Residue |
| A | TYR662 |
| A | ALA669 |
| A | ALA670 |
| A | ALA673 |
| site_id | AC2 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE MPD B 1679 |
| Chain | Residue |
| B | SER87 |
| B | HOH2045 |
| site_id | AC3 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE MPD B 1680 |
| Chain | Residue |
| B | ASP596 |
| B | TYR601 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CA B 1681 |
| Chain | Residue |
| B | GLY154 |
| B | ASP472 |
| B | ASP481 |
| B | HOH2103 |
| B | GLN153 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CA B 1682 |
| Chain | Residue |
| B | GLU648 |
| B | HOH2388 |
| B | HOH2389 |
| B | HOH2401 |
| B | HOH2402 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CA A 1683 |
| Chain | Residue |
| A | GLN153 |
| A | GLY154 |
| A | ASP472 |
| A | ASP481 |
| A | HOH2078 |
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 |
