7BRF
Structure of NADH complex of Thermotoga maritima alpha-glucuronidase at 2.15 Angstrom resolution
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000166 | molecular_function | nucleotide binding |
A | 0003824 | molecular_function | catalytic activity |
A | 0004553 | molecular_function | hydrolase activity, hydrolyzing O-glycosyl compounds |
A | 0005975 | biological_process | carbohydrate metabolic process |
A | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
A | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
A | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 26 |
Details | binding site for residue NAI A 500 |
Chain | Residue |
A | GLY7 |
A | TYR85 |
A | PRO86 |
A | TYR87 |
A | LEU138 |
A | THR158 |
A | ALA159 |
A | ASN160 |
A | PHE180 |
A | CSO181 |
A | ARG310 |
A | GLY9 |
A | HOH604 |
A | HOH607 |
A | HOH630 |
A | HOH649 |
A | HOH677 |
A | HOH731 |
A | HOH755 |
A | SER10 |
A | MET37 |
A | ASP38 |
A | VAL39 |
A | ARG43 |
A | THR83 |
A | ALA84 |