Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0003824 | molecular_function | catalytic activity |
A | 0005829 | cellular_component | cytosol |
A | 0006166 | biological_process | purine ribonucleoside salvage |
A | 0009116 | biological_process | nucleoside metabolic process |
A | 0016740 | molecular_function | transferase activity |
A | 0016757 | molecular_function | glycosyltransferase activity |
A | 0016763 | molecular_function | pentosyltransferase activity |
A | 0017061 | molecular_function | S-methyl-5-thioadenosine phosphorylase activity |
A | 0019509 | biological_process | L-methionine salvage from methylthioadenosine |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 15 |
Details | BINDING SITE FOR RESIDUE RHB A 301 |
Chain | Residue |
A | SER22 |
A | VAL278 |
A | RHB302 |
A | PO4303 |
A | CL305 |
A | HOH435 |
A | HOH574 |
A | TYR25 |
A | HIS65 |
A | PRO73 |
A | PHE179 |
A | ILE239 |
A | LEU242 |
A | MET243 |
A | GLN275 |
site_id | AC2 |
Number of Residues | 19 |
Details | BINDING SITE FOR RESIDUE RHB A 302 |
Chain | Residue |
A | ALA98 |
A | GLY100 |
A | PHE179 |
A | ILE196 |
A | GLY197 |
A | MET198 |
A | THR221 |
A | ASP222 |
A | PHE223 |
A | ASP224 |
A | CYS225 |
A | ASN229 |
A | ALA238 |
A | RHB301 |
A | CL304 |
A | HOH482 |
A | HOH575 |
A | HOH576 |
A | HOH579 |
site_id | AC3 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE PO4 A 303 |
Chain | Residue |
A | GLY21 |
A | SER22 |
A | ARG64 |
A | HIS65 |
A | SER97 |
A | ALA98 |
A | THR199 |
A | RHB301 |
A | HOH457 |
A | HOH482 |
site_id | AC4 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE CL A 304 |
Chain | Residue |
A | ASP222 |
A | ASN229 |
A | SER234 |
A | RHB302 |
site_id | AC5 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE CL A 305 |
Functional Information from PROSITE/UniProt
site_id | PS01240 |
Number of Residues | 41 |
Details | PNP_MTAP_2 Purine and other phosphorylases family 2 signature. LtrhGqgHrLtpseVpyrAn.IyAlktlGvry.IVsvSAvGSL |
Chain | Residue | Details |
A | LEU62-LEU102 | |