3T8I
Structural analysis of thermostable S. solfataricus purine-specific nucleoside hydrolase
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005829 | cellular_component | cytosol |
| A | 0006139 | biological_process | nucleobase-containing compound metabolic process |
| A | 0006152 | biological_process | purine nucleoside catabolic process |
| A | 0008477 | molecular_function | purine nucleosidase activity |
| A | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
| A | 0016799 | molecular_function | hydrolase activity, hydrolyzing N-glycosyl compounds |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0005829 | cellular_component | cytosol |
| B | 0006139 | biological_process | nucleobase-containing compound metabolic process |
| B | 0006152 | biological_process | purine nucleoside catabolic process |
| B | 0008477 | molecular_function | purine nucleosidase activity |
| B | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
| B | 0016799 | molecular_function | hydrolase activity, hydrolyzing N-glycosyl compounds |
| B | 0046872 | molecular_function | metal ion binding |
| C | 0005829 | cellular_component | cytosol |
| C | 0006139 | biological_process | nucleobase-containing compound metabolic process |
| C | 0006152 | biological_process | purine nucleoside catabolic process |
| C | 0008477 | molecular_function | purine nucleosidase activity |
| C | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
| C | 0016799 | molecular_function | hydrolase activity, hydrolyzing N-glycosyl compounds |
| C | 0046872 | molecular_function | metal ion binding |
| D | 0005829 | cellular_component | cytosol |
| D | 0006139 | biological_process | nucleobase-containing compound metabolic process |
| D | 0006152 | biological_process | purine nucleoside catabolic process |
| D | 0008477 | molecular_function | purine nucleosidase activity |
| D | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
| D | 0016799 | molecular_function | hydrolase activity, hydrolyzing N-glycosyl compounds |
| D | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE CA A 400 |
| Chain | Residue |
| A | ASP9 |
| A | ASP14 |
| A | ILE121 |
| A | ASP238 |
| A | GOL307 |
| A | HOH356 |
| A | HOH391 |
| site_id | AC2 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE GOL A 307 |
| Chain | Residue |
| A | ASN155 |
| A | GLU161 |
| A | PHE162 |
| A | ASN163 |
| A | ASP238 |
| A | HOH356 |
| A | HOH391 |
| A | CA400 |
| A | ILE121 |
| A | MET147 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL A 308 |
| Chain | Residue |
| A | PHE179 |
| A | ASP180 |
| A | ILE181 |
| A | ASN284 |
| A | GLU286 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE GOL A 309 |
| Chain | Residue |
| A | TRP275 |
| A | HOH357 |
| A | HOH375 |
| A | HOH411 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL A 310 |
| Chain | Residue |
| A | ASN155 |
| A | HOH316 |
| A | HOH371 |
| A | HOH422 |
| A | HOH448 |
| A | HOH916 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO A 311 |
| Chain | Residue |
| A | LEU69 |
| A | ASN71 |
| A | HOH433 |
| B | LYS172 |
| B | LEU263 |
| C | LYS266 |
| site_id | AC7 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE EDO A 312 |
| Chain | Residue |
| A | TRP72 |
| A | HOH393 |
| site_id | AC8 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE CA B 400 |
| Chain | Residue |
| B | ASP9 |
| B | ASP14 |
| B | ILE121 |
| B | ASP238 |
| B | GOL307 |
| B | HOH322 |
| B | HOH338 |
| site_id | AC9 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE GOL B 307 |
| Chain | Residue |
| B | ILE121 |
| B | MET147 |
| B | ASN155 |
| B | GLU161 |
| B | PHE162 |
| B | ASN163 |
| B | ASP238 |
| B | HOH322 |
| B | HOH338 |
| B | CA400 |
| site_id | BC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL B 308 |
| Chain | Residue |
| B | LYS282 |
| B | HOH333 |
| B | HOH380 |
| B | HOH405 |
| B | HOH652 |
| site_id | BC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL B 309 |
| Chain | Residue |
| B | PHE151 |
| B | TRP275 |
| B | HOH370 |
| B | HOH849 |
| C | LYS153 |
| site_id | BC3 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE GOL B 310 |
| Chain | Residue |
| B | VAL138 |
| B | LYS139 |
| B | VAL141 |
| B | LYS142 |
| B | GLY178 |
| B | PHE179 |
| B | ASP180 |
| B | HOH538 |
| B | HOH956 |
| site_id | BC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL B 311 |
| Chain | Residue |
| B | ARG2 |
| B | HIS246 |
| B | ASP247 |
| B | ASN248 |
| B | HOH909 |
| site_id | BC5 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL B 312 |
| Chain | Residue |
| B | ASN155 |
| B | TRP186 |
| B | HOH350 |
| B | HOH399 |
| B | HOH445 |
| B | HOH923 |
| B | HOH927 |
| site_id | BC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL B 313 |
| Chain | Residue |
| B | TRP72 |
| B | HOH354 |
| B | HOH395 |
| B | HOH396 |
| B | HOH638 |
| site_id | BC7 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE EDO B 314 |
| Chain | Residue |
| B | ARG198 |
| B | GLU201 |
| site_id | BC8 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE CA C 400 |
| Chain | Residue |
| C | GOL307 |
| C | HOH334 |
| C | HOH360 |
| C | ASP9 |
| C | ASP14 |
| C | ILE121 |
| C | ASP238 |
| site_id | BC9 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE GOL C 307 |
| Chain | Residue |
| C | ILE121 |
| C | MET147 |
| C | ASN155 |
| C | GLU161 |
| C | PHE162 |
| C | ASN163 |
| C | PRO237 |
| C | ASP238 |
| C | GOL308 |
| C | HOH334 |
| C | HOH360 |
| C | CA400 |
| site_id | CC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL C 308 |
| Chain | Residue |
| C | VAL75 |
| C | ASN155 |
| C | GOL307 |
| C | HOH763 |
| C | HOH836 |
| site_id | CC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE GOL C 309 |
| Chain | Residue |
| C | HOH601 |
| C | HOH872 |
| C | HOH936 |
| site_id | CC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE PEG C 310 |
| Chain | Residue |
| C | TRP72 |
| C | ARG73 |
| C | THR74 |
| site_id | CC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO C 311 |
| Chain | Residue |
| C | PHE179 |
| C | ILE181 |
| C | LEU256 |
| C | ASN284 |
| C | ALA285 |
| C | GLU286 |
| site_id | CC5 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE CA D 400 |
| Chain | Residue |
| D | ASP9 |
| D | ASP14 |
| D | ILE121 |
| D | ASP238 |
| D | GOL307 |
| D | HOH332 |
| D | HOH347 |
| site_id | CC6 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE GOL D 307 |
| Chain | Residue |
| D | ILE121 |
| D | MET147 |
| D | ASN155 |
| D | GLU161 |
| D | ASN163 |
| D | ASP238 |
| D | HOH332 |
| D | HOH347 |
| D | CA400 |
| site_id | CC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL D 308 |
| Chain | Residue |
| D | TRP72 |
| D | ARG73 |
| D | THR74 |
| D | HOH367 |
| D | HOH725 |
| site_id | CC8 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL D 309 |
| Chain | Residue |
| D | VAL75 |
| D | ASN155 |
| D | THR156 |
| D | PHE162 |
| D | TYR224 |
| D | HOH368 |
| D | HOH579 |
| site_id | CC9 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE PEG D 310 |
| Chain | Residue |
| C | ARG66 |
| C | LEU69 |
| D | TYR131 |
| D | ILE173 |
| D | ASP176 |
| D | ALA177 |
Functional Information from PROSITE/UniProt
| site_id | PS01247 |
| Number of Residues | 11 |
| Details | IUNH Inosine-uridine preferring nucleoside hydrolase family signature. DsDTAtDDTIA |
| Chain | Residue | Details |
| A | ASP7-ALA17 |
