7PR6
Crystal structure of E. coli beta-glucuronidase in complex with covalent inhibitor ME727
This is a non-PDB format compatible entry.
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| AAA | 0004553 | molecular_function | hydrolase activity, hydrolyzing O-glycosyl compounds |
| AAA | 0004566 | molecular_function | beta-glucuronidase activity |
| AAA | 0005829 | cellular_component | cytosol |
| AAA | 0005975 | biological_process | carbohydrate metabolic process |
| AAA | 0016787 | molecular_function | hydrolase activity |
| AAA | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
| AAA | 0030246 | molecular_function | carbohydrate binding |
| AAA | 0032991 | cellular_component | protein-containing complex |
| AAA | 0042802 | molecular_function | identical protein binding |
| BBB | 0004553 | molecular_function | hydrolase activity, hydrolyzing O-glycosyl compounds |
| BBB | 0004566 | molecular_function | beta-glucuronidase activity |
| BBB | 0005829 | cellular_component | cytosol |
| BBB | 0005975 | biological_process | carbohydrate metabolic process |
| BBB | 0016787 | molecular_function | hydrolase activity |
| BBB | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
| BBB | 0030246 | molecular_function | carbohydrate binding |
| BBB | 0032991 | cellular_component | protein-containing complex |
| BBB | 0042802 | molecular_function | identical protein binding |
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 |
| AAA | ASP399-GLU413 |
| site_id | PS00719 |
| Number of Residues | 26 |
| Details | GLYCOSYL_HYDROL_F2_1 Glycosyl hydrolases family 2 signature 1. NsYRTSHYPyaeeMLdwaDehGIVVI |
| Chain | Residue | Details |
| AAA | ASN324-ILE349 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| 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 | 2 |
| 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 | 2 |
| 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 | 14 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"21051639","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"3K4D","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
