5WCZ
Crystal Structure of Wild-Type MalL from Bacillus subtilis with TS analogue 1-deoxynojirimycin
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004556 | molecular_function | alpha-amylase activity |
| A | 0004574 | molecular_function | oligo-1,6-glucosidase activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005975 | biological_process | carbohydrate metabolic process |
| A | 0009313 | biological_process | oligosaccharide catabolic process |
| A | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0004556 | molecular_function | alpha-amylase activity |
| B | 0004574 | molecular_function | oligo-1,6-glucosidase activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005975 | biological_process | carbohydrate metabolic process |
| B | 0009313 | biological_process | oligosaccharide catabolic process |
| B | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
| B | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 13 |
| Details | binding site for residue NOJ A 601 |
| Chain | Residue |
| A | ASP59 |
| A | HIS331 |
| A | ASP332 |
| A | ARG418 |
| A | HOH932 |
| A | TYR62 |
| A | HIS102 |
| A | PHE144 |
| A | PHE163 |
| A | ARG197 |
| A | ASP199 |
| A | VAL200 |
| A | GLU255 |
| site_id | AC2 |
| Number of Residues | 8 |
| Details | binding site for residue GOL A 602 |
| Chain | Residue |
| A | LYS296 |
| A | ASP332 |
| A | GLU389 |
| A | ARG418 |
| A | HOH760 |
| A | HOH1006 |
| A | HOH1043 |
| A | HOH1192 |
| site_id | AC3 |
| Number of Residues | 7 |
| Details | binding site for residue GOL A 603 |
| Chain | Residue |
| A | HIS283 |
| A | TRP314 |
| A | GLN315 |
| A | ASN324 |
| A | THR325 |
| A | HOH756 |
| A | HOH896 |
| site_id | AC4 |
| Number of Residues | 13 |
| Details | binding site for residue NOJ B 601 |
| Chain | Residue |
| B | ASP59 |
| B | TYR62 |
| B | HIS102 |
| B | PHE144 |
| B | PHE163 |
| B | ARG197 |
| B | ASP199 |
| B | VAL200 |
| B | GLU255 |
| B | HIS331 |
| B | ASP332 |
| B | ARG418 |
| B | HOH904 |
| site_id | AC5 |
| Number of Residues | 8 |
| Details | binding site for residue GOL B 602 |
| Chain | Residue |
| B | HIS283 |
| B | MET311 |
| B | TRP314 |
| B | GLN315 |
| B | ASN324 |
| B | THR325 |
| B | LEU326 |
| B | TYR327 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | ACT_SITE: Nucleophile => ECO:0000250 |
| Chain | Residue | Details |
| A | ASP199 | |
| B | ASP199 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | ACT_SITE: Proton donor => ECO:0000250 |
| Chain | Residue | Details |
| A | GLU255 | |
| B | GLU255 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 10 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:24015933, ECO:0007744|PDB:4M8U, ECO:0007744|PDB:4MB1 |
| Chain | Residue | Details |
| A | ASP20 | |
| B | ASP28 | |
| A | ASN22 | |
| A | ASP24 | |
| A | PHE26 | |
| A | ASP28 | |
| B | ASP20 | |
| B | ASN22 | |
| B | ASP24 | |
| B | PHE26 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | SITE: Transition state stabilizer => ECO:0000250 |
| Chain | Residue | Details |
| A | ASP332 | |
| B | ASP332 |
