6LD0
Structure of Bifidobacterium dentium beta-glucuronidase complexed with C6-hexyl uronic isofagomine
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004553 | molecular_function | hydrolase activity, hydrolyzing O-glycosyl compounds |
A | 0004565 | molecular_function | beta-galactosidase activity |
A | 0004566 | molecular_function | beta-glucuronidase activity |
A | 0005975 | biological_process | carbohydrate metabolic process |
A | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
A | 0030246 | molecular_function | carbohydrate binding |
B | 0004553 | molecular_function | hydrolase activity, hydrolyzing O-glycosyl compounds |
B | 0004565 | molecular_function | beta-galactosidase activity |
B | 0004566 | molecular_function | beta-glucuronidase activity |
B | 0005975 | biological_process | carbohydrate metabolic process |
B | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
B | 0030246 | molecular_function | carbohydrate binding |
C | 0004553 | molecular_function | hydrolase activity, hydrolyzing O-glycosyl compounds |
C | 0004565 | molecular_function | beta-galactosidase activity |
C | 0004566 | molecular_function | beta-glucuronidase activity |
C | 0005975 | biological_process | carbohydrate metabolic process |
C | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
C | 0030246 | molecular_function | carbohydrate binding |
D | 0004553 | molecular_function | hydrolase activity, hydrolyzing O-glycosyl compounds |
D | 0004565 | molecular_function | beta-galactosidase activity |
D | 0004566 | molecular_function | beta-glucuronidase activity |
D | 0005975 | biological_process | carbohydrate metabolic process |
D | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
D | 0030246 | molecular_function | carbohydrate binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 14 |
Details | binding site for residue E8X A 701 |
Chain | Residue |
A | ASP179 |
A | ASN636 |
A | LYS638 |
A | HOH830 |
A | HOH912 |
D | ASN157 |
A | HIS413 |
A | GLU479 |
A | GLN519 |
A | TYR539 |
A | TYR543 |
A | GLU574 |
A | TRP619 |
A | ARG632 |
site_id | AC2 |
Number of Residues | 15 |
Details | binding site for residue E8X B 701 |
Chain | Residue |
B | MET153 |
B | ASP179 |
B | HIS413 |
B | GLU479 |
B | GLN519 |
B | TYR539 |
B | TYR543 |
B | GLU574 |
B | TRP619 |
B | ARG632 |
B | ASN636 |
B | LYS638 |
B | HOH840 |
B | HOH930 |
C | ASN157 |
site_id | AC3 |
Number of Residues | 15 |
Details | binding site for residue E8X C 701 |
Chain | Residue |
B | ASN157 |
C | ASP179 |
C | HIS413 |
C | ASN478 |
C | GLU479 |
C | GLN519 |
C | TYR539 |
C | TYR543 |
C | GLU574 |
C | TRP619 |
C | ARG632 |
C | ASN636 |
C | LYS638 |
C | HOH848 |
C | HOH856 |
site_id | AC4 |
Number of Residues | 14 |
Details | binding site for residue E8X D 701 |
Chain | Residue |
A | ASN157 |
D | ASP179 |
D | HIS413 |
D | GLU479 |
D | GLN519 |
D | TYR539 |
D | TYR543 |
D | GLU574 |
D | TRP619 |
D | ARG632 |
D | ASN636 |
D | LYS638 |
D | HOH814 |
D | HOH903 |
Functional Information from PROSITE/UniProt
site_id | PS00608 |
Number of Residues | 15 |
Details | GLYCOSYL_HYDROL_F2_2 Glycosyl hydrolases family 2 acid/base catalyst. DKNHPCIVMWSia.NE |
Chain | Residue | Details |
A | ASP465-GLU479 |
site_id | PS00719 |
Number of Residues | 26 |
Details | GLYCOSYL_HYDROL_F2_1 Glycosyl hydrolases family 2 signature 1. NsFRTSHYPyaesMYdlcDreGIVII |
Chain | Residue | Details |
A | ASN407-ILE432 |