8OHX
Crystal structure of Beta-glucuronidase from Escherichia coli in complex with siastatin B derived inhibitor
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 | 0019391 | biological_process | glucuronoside catabolic process |
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 | 0019391 | biological_process | glucuronoside catabolic process |
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 | 2 |
Details | ACT_SITE: Proton donor => ECO:0000305|PubMed:21051639 |
Chain | Residue | Details |
AAA | GLU413 | |
BBB | GLU413 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | ACT_SITE: Nucleophile => ECO:0000269|PubMed:35881786, ECO:0000305|PubMed:21051639 |
Chain | Residue | Details |
AAA | GLU504 | |
BBB | GLU504 |
site_id | SWS_FT_FI3 |
Number of Residues | 14 |
Details | BINDING: BINDING => ECO:0000305|PubMed:21051639, ECO:0007744|PDB:3K4D |
Chain | Residue | Details |
AAA | ASP163 | |
BBB | ASN466 | |
BBB | TYR472 | |
BBB | GLU504 | |
BBB | TRP549 | |
BBB | LYS568 | |
AAA | ASN412 | |
AAA | ASN466 | |
AAA | TYR472 | |
AAA | GLU504 | |
AAA | TRP549 | |
AAA | LYS568 | |
BBB | ASP163 | |
BBB | ASN412 |