5NS8
Crystal structure of beta-glucosidase BglM-G1 mutant H75R from marine metagenome in complex with inhibitor 1-Deoxynojirimycin
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004553 | molecular_function | hydrolase activity, hydrolyzing O-glycosyl compounds |
| A | 0005975 | biological_process | carbohydrate metabolic process |
| A | 0008422 | molecular_function | beta-glucosidase activity |
| A | 0030245 | biological_process | cellulose catabolic process |
| B | 0004553 | molecular_function | hydrolase activity, hydrolyzing O-glycosyl compounds |
| B | 0005975 | biological_process | carbohydrate metabolic process |
| B | 0008422 | molecular_function | beta-glucosidase activity |
| B | 0030245 | biological_process | cellulose catabolic process |
| C | 0004553 | molecular_function | hydrolase activity, hydrolyzing O-glycosyl compounds |
| C | 0005975 | biological_process | carbohydrate metabolic process |
| C | 0008422 | molecular_function | beta-glucosidase activity |
| C | 0030245 | biological_process | cellulose catabolic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 2 |
| Details | binding site for residue SO4 A 501 |
| Chain | Residue |
| A | ARG293 |
| A | HIS325 |
| site_id | AC2 |
| Number of Residues | 2 |
| Details | binding site for residue SO4 A 502 |
| Chain | Residue |
| A | TRP68 |
| C | GLU108 |
| site_id | AC3 |
| Number of Residues | 9 |
| Details | binding site for residue GOL A 503 |
| Chain | Residue |
| A | HOH719 |
| C | TRP354 |
| C | ASP355 |
| C | GOL505 |
| A | PRO273 |
| A | GLY274 |
| A | ASP275 |
| A | MET276 |
| A | GLU277 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | binding site for residue GOL A 504 |
| Chain | Residue |
| A | TYR175 |
| A | LYS303 |
| A | PRO304 |
| A | LEU305 |
| A | TYR307 |
| A | LYS308 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | binding site for residue GOL A 505 |
| Chain | Residue |
| A | LEU283 |
| A | LYS341 |
| A | PRO342 |
| A | LYS343 |
| A | HOH671 |
| C | ASN314 |
| site_id | AC6 |
| Number of Residues | 11 |
| Details | binding site for residue NOJ A 506 |
| Chain | Residue |
| A | GLN18 |
| A | HIS119 |
| A | ASN163 |
| A | GLU164 |
| A | TYR291 |
| A | TRP322 |
| A | GLU349 |
| A | TRP395 |
| A | GLU402 |
| A | TRP403 |
| A | PHE411 |
| site_id | AC7 |
| Number of Residues | 7 |
| Details | binding site for residue SO4 B 501 |
| Chain | Residue |
| B | LYS254 |
| B | LYS256 |
| B | VAL310 |
| B | THR311 |
| B | HOH623 |
| B | HOH646 |
| B | HOH845 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | binding site for residue SO4 B 502 |
| Chain | Residue |
| A | GLU108 |
| B | LEU65 |
| B | TRP68 |
| B | PRO425 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | binding site for residue SO4 B 503 |
| Chain | Residue |
| B | ARG293 |
| B | HIS325 |
| B | HOH649 |
| B | HOH851 |
| site_id | AD1 |
| Number of Residues | 6 |
| Details | binding site for residue GOL B 504 |
| Chain | Residue |
| B | ASP6 |
| B | MET7 |
| B | LYS383 |
| B | PRO388 |
| B | ILE389 |
| B | SER390 |
| site_id | AD2 |
| Number of Residues | 8 |
| Details | binding site for residue GOL B 505 |
| Chain | Residue |
| B | TYR175 |
| B | LYS303 |
| B | PRO304 |
| B | LEU305 |
| B | TYR307 |
| B | LYS308 |
| B | HOH624 |
| B | HOH860 |
| site_id | AD3 |
| Number of Residues | 6 |
| Details | binding site for residue GOL B 506 |
| Chain | Residue |
| B | LEU283 |
| B | ASN314 |
| B | LYS341 |
| B | PRO342 |
| B | LYS343 |
| B | HOH692 |
| site_id | AD4 |
| Number of Residues | 3 |
| Details | binding site for residue GOL B 507 |
| Chain | Residue |
| B | ALA326 |
| B | GLN327 |
| B | ARG374 |
| site_id | AD5 |
| Number of Residues | 7 |
| Details | binding site for residue GOL B 508 |
| Chain | Residue |
| B | ALA255 |
| B | THR318 |
| B | GLY319 |
| B | GLY321 |
| B | HOH670 |
| B | HOH720 |
| B | HOH825 |
| site_id | AD6 |
| Number of Residues | 10 |
| Details | binding site for residue GOL B 509 |
| Chain | Residue |
| B | PRO273 |
| B | GLY274 |
| B | ASP275 |
| B | MET276 |
| B | GLU277 |
| B | GLY319 |
| B | TRP354 |
| B | ASP355 |
| B | HOH710 |
| B | HOH772 |
| site_id | AD7 |
| Number of Residues | 12 |
| Details | binding site for residue NOJ B 510 |
| Chain | Residue |
| B | GLU402 |
| B | TRP403 |
| B | PHE411 |
| B | HOH830 |
| B | GLN18 |
| B | HIS119 |
| B | ASN163 |
| B | GLU164 |
| B | TYR291 |
| B | TRP322 |
| B | GLU349 |
| B | TRP395 |
| site_id | AD8 |
| Number of Residues | 3 |
| Details | binding site for residue SO4 C 501 |
| Chain | Residue |
| C | ARG293 |
| C | HIS325 |
| C | HOH806 |
| site_id | AD9 |
| Number of Residues | 4 |
| Details | binding site for residue SO4 C 502 |
| Chain | Residue |
| A | LYS254 |
| A | LYS256 |
| C | VAL310 |
| C | THR311 |
| site_id | AE1 |
| Number of Residues | 7 |
| Details | binding site for residue GOL C 503 |
| Chain | Residue |
| C | TYR175 |
| C | ALA302 |
| C | LYS303 |
| C | PRO304 |
| C | LEU305 |
| C | TYR307 |
| C | HOH604 |
| site_id | AE2 |
| Number of Residues | 6 |
| Details | binding site for residue GOL C 504 |
| Chain | Residue |
| C | PHE253 |
| C | PRO282 |
| C | LEU283 |
| C | PRO342 |
| C | LYS343 |
| C | HOH680 |
| site_id | AE3 |
| Number of Residues | 8 |
| Details | binding site for residue GOL C 505 |
| Chain | Residue |
| A | ALA255 |
| A | GLU277 |
| A | GOL503 |
| A | HOH630 |
| C | THR318 |
| C | GLY321 |
| C | HOH602 |
| C | HOH647 |
| site_id | AE4 |
| Number of Residues | 11 |
| Details | binding site for residue NOJ C 506 |
| Chain | Residue |
| C | GLN18 |
| C | HIS119 |
| C | ASN163 |
| C | GLU164 |
| C | TYR291 |
| C | TRP322 |
| C | GLU349 |
| C | TRP395 |
| C | GLU402 |
| C | TRP403 |
| C | PHE411 |
Functional Information from PROSITE/UniProt
| site_id | PS00653 |
| Number of Residues | 15 |
| Details | GLYCOSYL_HYDROL_F1_2 Glycosyl hydrolases family 1 N-terminal signature. FtWGvStSSYQiEgA |
| Chain | Residue | Details |
| A | PHE8-ALA22 |
