3OTX
Crystal Structure of Trypanosoma brucei rhodesiense Adenosine Kinase Complexed with Inhibitor AP5A
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004001 | molecular_function | adenosine kinase activity |
| A | 0005524 | molecular_function | ATP binding |
| A | 0005634 | cellular_component | nucleus |
| A | 0005654 | cellular_component | nucleoplasm |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0006144 | biological_process | purine nucleobase metabolic process |
| A | 0006166 | biological_process | purine ribonucleoside salvage |
| A | 0009152 | biological_process | purine ribonucleotide biosynthetic process |
| A | 0016301 | molecular_function | kinase activity |
| A | 0020015 | cellular_component | glycosome |
| A | 0044209 | biological_process | AMP salvage |
| A | 0097014 | cellular_component | ciliary plasm |
| B | 0004001 | molecular_function | adenosine kinase activity |
| B | 0005524 | molecular_function | ATP binding |
| B | 0005634 | cellular_component | nucleus |
| B | 0005654 | cellular_component | nucleoplasm |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005829 | cellular_component | cytosol |
| B | 0006144 | biological_process | purine nucleobase metabolic process |
| B | 0006166 | biological_process | purine ribonucleoside salvage |
| B | 0009152 | biological_process | purine ribonucleotide biosynthetic process |
| B | 0016301 | molecular_function | kinase activity |
| B | 0020015 | cellular_component | glycosome |
| B | 0044209 | biological_process | AMP salvage |
| B | 0097014 | cellular_component | ciliary plasm |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 50 |
| Details | BINDING SITE FOR RESIDUE AP5 A 346 |
| Chain | Residue |
| A | CYS12 |
| A | CYS123 |
| A | ARG132 |
| A | ALA136 |
| A | PHE169 |
| A | ASN222 |
| A | THR264 |
| A | ARG265 |
| A | ASP266 |
| A | ILE267 |
| A | THR270 |
| A | ASN13 |
| A | VAL283 |
| A | GLN288 |
| A | GLY296 |
| A | ALA297 |
| A | GLY298 |
| A | ASP299 |
| A | HIS323 |
| A | ALA326 |
| A | GLN327 |
| A | ILE330 |
| A | LEU15 |
| A | NA347 |
| A | HOH355 |
| A | HOH357 |
| A | HOH364 |
| A | HOH368 |
| A | HOH384 |
| A | HOH448 |
| A | HOH449 |
| A | HOH452 |
| A | HOH456 |
| A | ASP17 |
| A | HOH459 |
| A | HOH464 |
| A | HOH506 |
| A | HOH515 |
| A | HOH518 |
| A | HOH564 |
| A | HOH585 |
| A | HOH637 |
| A | HOH638 |
| A | HOH642 |
| A | LEU39 |
| A | HOH685 |
| A | GLY62 |
| A | GLY63 |
| A | SER64 |
| A | ASN67 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE NA A 347 |
| Chain | Residue |
| A | ASP299 |
| A | AP5346 |
| A | HOH384 |
| A | HOH472 |
| A | HOH638 |
| A | HOH639 |
| site_id | AC3 |
| Number of Residues | 49 |
| Details | BINDING SITE FOR RESIDUE AP5 B 346 |
| Chain | Residue |
| B | HOH437 |
| B | HOH448 |
| B | HOH555 |
| B | HOH581 |
| B | HOH583 |
| B | HOH631 |
| A | HIS105 |
| B | CYS12 |
| B | ASN13 |
| B | LEU15 |
| B | ASP17 |
| B | LEU39 |
| B | GLY62 |
| B | GLY63 |
| B | SER64 |
| B | ASN67 |
| B | ARG132 |
| B | ALA136 |
| B | LEU138 |
| B | PHE169 |
| B | ASN222 |
| B | THR264 |
| B | ARG265 |
| B | ASP266 |
| B | ILE267 |
| B | THR270 |
| B | VAL283 |
| B | GLN288 |
| B | GLY296 |
| B | ALA297 |
| B | GLY298 |
| B | ASP299 |
| B | HIS323 |
| B | ALA326 |
| B | GLN327 |
| B | ILE330 |
| B | NA347 |
| B | HOH367 |
| B | HOH385 |
| B | HOH389 |
| B | HOH396 |
| B | HOH400 |
| B | HOH404 |
| B | HOH409 |
| B | HOH417 |
| B | HOH419 |
| B | HOH420 |
| B | HOH424 |
| B | HOH426 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE NA B 347 |
| Chain | Residue |
| B | ASP299 |
| B | AP5346 |
| B | HOH417 |
| B | HOH630 |
| B | HOH631 |
| B | HOH632 |
