6LEG
Structure of E. coli beta-glucuronidase complex with uronic isofagomine
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004553 | molecular_function | hydrolase activity, hydrolyzing O-glycosyl compounds |
| A | 0004566 | molecular_function | beta-glucuronidase activity |
| A | 0005829 | cellular_component | cytosol |
| A | 0005975 | biological_process | carbohydrate metabolic process |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
| A | 0030246 | molecular_function | carbohydrate binding |
| A | 0032991 | cellular_component | protein-containing complex |
| A | 0042802 | molecular_function | identical protein binding |
| B | 0004553 | molecular_function | hydrolase activity, hydrolyzing O-glycosyl compounds |
| B | 0004566 | molecular_function | beta-glucuronidase activity |
| B | 0005829 | cellular_component | cytosol |
| B | 0005975 | biological_process | carbohydrate metabolic process |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
| B | 0030246 | molecular_function | carbohydrate binding |
| B | 0032991 | cellular_component | protein-containing complex |
| B | 0042802 | molecular_function | identical protein binding |
| C | 0004553 | molecular_function | hydrolase activity, hydrolyzing O-glycosyl compounds |
| C | 0004566 | molecular_function | beta-glucuronidase activity |
| C | 0005829 | cellular_component | cytosol |
| C | 0005975 | biological_process | carbohydrate metabolic process |
| C | 0016787 | molecular_function | hydrolase activity |
| C | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
| C | 0030246 | molecular_function | carbohydrate binding |
| C | 0032991 | cellular_component | protein-containing complex |
| C | 0042802 | molecular_function | identical protein binding |
| D | 0004553 | molecular_function | hydrolase activity, hydrolyzing O-glycosyl compounds |
| D | 0004566 | molecular_function | beta-glucuronidase activity |
| D | 0005829 | cellular_component | cytosol |
| D | 0005975 | biological_process | carbohydrate metabolic process |
| D | 0016787 | molecular_function | hydrolase activity |
| D | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
| D | 0030246 | molecular_function | carbohydrate binding |
| D | 0032991 | cellular_component | protein-containing complex |
| D | 0042802 | molecular_function | identical protein binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 9 |
| Details | binding site for residue SJ5 A 701 |
| Chain | Residue |
| A | ASP163 |
| A | HIS330 |
| A | GLU413 |
| A | TYR468 |
| A | TYR472 |
| A | GLU504 |
| A | TRP549 |
| A | ASN566 |
| A | LYS568 |
| site_id | AC2 |
| Number of Residues | 11 |
| Details | binding site for residue SJ5 B 701 |
| Chain | Residue |
| B | ASP163 |
| B | HIS330 |
| B | GLU413 |
| B | TYR468 |
| B | TYR472 |
| B | GLU504 |
| B | TRP549 |
| B | ARG562 |
| B | ASN566 |
| B | LYS568 |
| B | HOH835 |
| site_id | AC3 |
| Number of Residues | 11 |
| Details | binding site for residue SJ5 C 701 |
| Chain | Residue |
| C | ASP163 |
| C | HIS330 |
| C | ILE363 |
| C | GLU413 |
| C | TYR468 |
| C | TYR472 |
| C | GLU504 |
| C | TRP549 |
| C | ASN566 |
| C | LYS568 |
| C | HOH810 |
| site_id | AC4 |
| Number of Residues | 9 |
| Details | binding site for residue SJ5 D 701 |
| Chain | Residue |
| D | ASP163 |
| D | HIS330 |
| D | GLU413 |
| D | TYR468 |
| D | TYR472 |
| D | GLU504 |
| D | TRP549 |
| D | ASN566 |
| D | LYS568 |
Functional Information from PROSITE/UniProt
| site_id | PS00608 |
| Number of Residues | 15 |
| Details | GLYCOSYL_HYDROL_F2_2 Glycosyl hydrolases family 2 acid/base catalyst. DKNHPSVVMWSia.NE |
| Chain | Residue | Details |
| A | ASP399-GLU413 |
| site_id | PS00719 |
| Number of Residues | 26 |
| Details | GLYCOSYL_HYDROL_F2_1 Glycosyl hydrolases family 2 signature 1. NsYRTSHYPyaeeMLdwaDehGIVVI |
| Chain | Residue | Details |
| A | ASN324-ILE349 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 8 |
| Details | Motif: {"description":"N-K motif","evidences":[{"source":"PubMed","id":"26364932","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | Active site: {"description":"Proton donor","evidences":[{"source":"PubMed","id":"21051639","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | Active site: {"description":"Nucleophile","evidences":[{"source":"PubMed","id":"35881786","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"21051639","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 28 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"21051639","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"3K4D","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
