7KGY
Beta-glucuronidase from Faecalibacterium prausnitzii bound to the inhibitor UNC10201652-glucuronide
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 |
B | 0004553 | molecular_function | hydrolase activity, hydrolyzing O-glycosyl compounds |
B | 0005975 | biological_process | carbohydrate metabolic process |
C | 0004553 | molecular_function | hydrolase activity, hydrolyzing O-glycosyl compounds |
C | 0005975 | biological_process | carbohydrate metabolic process |
D | 0004553 | molecular_function | hydrolase activity, hydrolyzing O-glycosyl compounds |
D | 0005975 | biological_process | carbohydrate metabolic process |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 16 |
Details | binding site for residue I9G A 701 |
Chain | Residue |
A | ASP167 |
A | PHE563 |
A | ARG571 |
A | ASN575 |
A | LYS577 |
A | HOH855 |
A | HOH1094 |
B | ILE569 |
A | HIS334 |
A | ASN418 |
A | GLU419 |
A | ASN473 |
A | TYR475 |
A | TYR479 |
A | GLU513 |
A | TRP558 |
site_id | AC2 |
Number of Residues | 11 |
Details | binding site for residue GOL A 702 |
Chain | Residue |
A | GLU301 |
A | ASP302 |
A | GLY309 |
A | LEU310 |
A | ASP311 |
A | VAL315 |
A | ASP318 |
A | ARG584 |
A | HOH813 |
A | HOH882 |
A | HOH1033 |
site_id | AC3 |
Number of Residues | 16 |
Details | binding site for residue I9G B 701 |
Chain | Residue |
A | ILE569 |
B | ASP167 |
B | HIS334 |
B | ASN418 |
B | GLU419 |
B | ASN473 |
B | TYR475 |
B | TYR479 |
B | GLU513 |
B | TRP558 |
B | PHE563 |
B | ARG571 |
B | ASN575 |
B | LYS577 |
B | HOH863 |
B | HOH1021 |
site_id | AC4 |
Number of Residues | 11 |
Details | binding site for residue GOL B 702 |
Chain | Residue |
B | GLU301 |
B | ASP302 |
B | GLY309 |
B | LEU310 |
B | ASP311 |
B | VAL315 |
B | ASP318 |
B | ARG584 |
B | HOH820 |
B | HOH897 |
B | HOH929 |
site_id | AC5 |
Number of Residues | 16 |
Details | binding site for residue I9G C 701 |
Chain | Residue |
C | ASP167 |
C | HIS334 |
C | ASN418 |
C | GLU419 |
C | ASN473 |
C | TYR475 |
C | TYR479 |
C | GLU513 |
C | TRP558 |
C | PHE563 |
C | ARG571 |
C | ASN575 |
C | LYS577 |
C | HOH843 |
C | HOH954 |
D | ILE569 |
site_id | AC6 |
Number of Residues | 16 |
Details | binding site for residue I9G D 701 |
Chain | Residue |
C | ILE569 |
D | ASP167 |
D | HIS334 |
D | ASN418 |
D | GLU419 |
D | ASN473 |
D | TYR475 |
D | TYR479 |
D | GLU513 |
D | TRP558 |
D | PHE563 |
D | ARG571 |
D | ASN575 |
D | LYS577 |
D | HOH850 |
D | HOH962 |
site_id | AC7 |
Number of Residues | 10 |
Details | binding site for residue GOL D 702 |
Chain | Residue |
D | GLU301 |
D | ASP302 |
D | GLY309 |
D | LEU310 |
D | ASP311 |
D | THR314 |
D | VAL315 |
D | ASP318 |
D | HOH802 |
D | HOH836 |
Functional Information from PROSITE/UniProt
site_id | PS00719 |
Number of Residues | 26 |
Details | GLYCOSYL_HYDROL_F2_1 Glycosyl hydrolases family 2 signature 1. NcFRTSHYPyaeeLYqmaDeeGFLII |
Chain | Residue | Details |
A | ASN328-ILE353 |