3UAX
Crystal structure of adenosine phosphorylase from Bacillus cereus complexed with inosine
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0003824 | molecular_function | catalytic activity |
A | 0004731 | molecular_function | purine-nucleoside phosphorylase activity |
A | 0004850 | molecular_function | uridine phosphorylase activity |
A | 0005829 | cellular_component | cytosol |
A | 0006139 | biological_process | nucleobase-containing compound metabolic process |
A | 0006152 | biological_process | purine nucleoside catabolic process |
A | 0006218 | biological_process | uridine catabolic process |
A | 0009116 | biological_process | nucleoside metabolic process |
A | 0009164 | biological_process | nucleoside catabolic process |
A | 0016757 | molecular_function | glycosyltransferase activity |
A | 0016763 | molecular_function | pentosyltransferase activity |
A | 0042278 | biological_process | purine nucleoside metabolic process |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 17 |
Details | BINDING SITE FOR RESIDUE NOS A 236 |
Chain | Residue |
A | HIS4 |
A | GLU179 |
A | MET180 |
A | GLU181 |
A | SO4237 |
A | HOH262 |
A | HOH304 |
A | HOH313 |
A | HOH372 |
A | ARG43 |
A | MET64 |
A | ARG87 |
A | THR90 |
A | CYS91 |
A | GLY92 |
A | PHE159 |
A | VAL178 |
site_id | AC2 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE SO4 A 237 |
Chain | Residue |
A | GLY20 |
A | ARG43 |
A | ARG87 |
A | GLY89 |
A | THR90 |
A | NOS236 |
A | HOH263 |
A | HOH303 |
site_id | AC3 |
Number of Residues | 13 |
Details | BINDING SITE FOR RESIDUE GOL A 238 |
Chain | Residue |
A | THR119 |
A | TYR160 |
A | ARG161 |
A | GLU162 |
A | LYS169 |
A | TYR173 |
A | LYS191 |
A | HOH241 |
A | HOH249 |
A | HOH260 |
A | HOH443 |
A | HOH444 |
A | HOH450 |
Functional Information from PROSITE/UniProt
site_id | PS01232 |
Number of Residues | 16 |
Details | PNP_UDP_1 Purine and other phosphorylases family 1 signature. GtGMGvPSiSIyvnEL |
Chain | Residue | Details |
A | GLY61-LEU76 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 1 |
Details | ACT_SITE: Proton donor => ECO:0000255|HAMAP-Rule:MF_01627 |
Chain | Residue | Details |
A | ASP204 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000250|UniProtKB:P50389 |
Chain | Residue | Details |
A | HIS4 | |
A | ARG43 |
site_id | SWS_FT_FI3 |
Number of Residues | 6 |
Details | BINDING: in other chain => ECO:0000250|UniProtKB:P50389 |
Chain | Residue | Details |
A | GLY20 | |
A | ARG24 | |
A | ARG87 | |
A | GLU162 | |
A | GLU179 | |
A | SER203 |
site_id | SWS_FT_FI4 |
Number of Residues | 1 |
Details | SITE: Important for catalytic activity => ECO:0000255|HAMAP-Rule:MF_01627 |
Chain | Residue | Details |
A | ARG217 |