3HN3
Human beta-glucuronidase at 1.7 A resolution
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 |
D | 0004553 | molecular_function | hydrolase activity, hydrolyzing O-glycosyl compounds |
D | 0005975 | biological_process | carbohydrate metabolic process |
E | 0004553 | molecular_function | hydrolase activity, hydrolyzing O-glycosyl compounds |
E | 0005975 | biological_process | carbohydrate metabolic process |
Functional Information from PROSITE/UniProt
site_id | PS00608 |
Number of Residues | 15 |
Details | GLYCOSYL_HYDROL_F2_2 Glycosyl hydrolases family 2 acid/base catalyst. DKNHPAVVMWSva.NE |
Chain | Residue | Details |
A | ASP437-GLU451 |
site_id | PS00719 |
Number of Residues | 26 |
Details | GLYCOSYL_HYDROL_F2_1 Glycosyl hydrolases family 2 signature 1. NaFRTSHYPyaeeVMqmcDryGIVVI |
Chain | Residue | Details |
A | ASN379-ILE404 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 4 |
Details | ACT_SITE: Proton donor |
Chain | Residue | Details |
A | GLU451 | |
B | GLU451 | |
D | GLU451 | |
E | GLU451 |
site_id | SWS_FT_FI2 |
Number of Residues | 8 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19159218 |
Chain | Residue | Details |
A | ASN173 | |
A | ASN631 | |
B | ASN173 | |
B | ASN631 | |
D | ASN173 | |
D | ASN631 | |
E | ASN173 | |
E | ASN631 |
site_id | SWS_FT_FI3 |
Number of Residues | 4 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:12754519, ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19159218 |
Chain | Residue | Details |
A | ASN272 | |
B | ASN272 | |
D | ASN272 | |
E | ASN272 |
site_id | SWS_FT_FI4 |
Number of Residues | 4 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine |
Chain | Residue | Details |
A | ASN420 | |
B | ASN420 | |
D | ASN420 | |
E | ASN420 |
Catalytic Information from CSA
site_id | MCSA1 |
Number of Residues | 4 |
Details | M-CSA 423 |
Chain | Residue | Details |
A | ASP207 | electrostatic stabiliser |
A | GLU451 | proton shuttle (general acid/base) |
A | TYR504 | electrostatic stabiliser |
A | GLU540 | covalent catalysis |
site_id | MCSA2 |
Number of Residues | 4 |
Details | M-CSA 423 |
Chain | Residue | Details |
B | ASP207 | electrostatic stabiliser |
B | GLU451 | proton shuttle (general acid/base) |
B | TYR504 | electrostatic stabiliser |
B | GLU540 | covalent catalysis |
site_id | MCSA3 |
Number of Residues | 4 |
Details | M-CSA 423 |
Chain | Residue | Details |
D | ASP207 | electrostatic stabiliser |
D | GLU451 | proton shuttle (general acid/base) |
D | TYR504 | electrostatic stabiliser |
D | GLU540 | covalent catalysis |
site_id | MCSA4 |
Number of Residues | 4 |
Details | M-CSA 423 |
Chain | Residue | Details |
E | ASP207 | electrostatic stabiliser |
E | GLU451 | proton shuttle (general acid/base) |
E | TYR504 | electrostatic stabiliser |
E | GLU540 | covalent catalysis |