1UOU
Crystal structure of human thymidine phosphorylase in complex with a small molecule inhibitor
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0001525 | biological_process | angiogenesis |
| A | 0004645 | molecular_function | 1,4-alpha-oligoglucan phosphorylase activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005829 | cellular_component | cytosol |
| A | 0006206 | biological_process | pyrimidine nucleobase metabolic process |
| A | 0006213 | biological_process | pyrimidine nucleoside metabolic process |
| A | 0006935 | biological_process | chemotaxis |
| A | 0007165 | biological_process | signal transduction |
| A | 0008083 | molecular_function | growth factor activity |
| A | 0009032 | molecular_function | thymidine phosphorylase activity |
| A | 0016154 | molecular_function | pyrimidine-nucleoside phosphorylase activity |
| A | 0016740 | molecular_function | transferase activity |
| A | 0016757 | molecular_function | glycosyltransferase activity |
| A | 0016763 | molecular_function | pentosyltransferase activity |
| A | 0030154 | biological_process | cell differentiation |
| A | 0042803 | molecular_function | protein homodimerization activity |
| A | 0046074 | biological_process | dTMP catabolic process |
| A | 0055086 | biological_process | nucleobase-containing small molecule metabolic process |
| A | 0072527 | biological_process | pyrimidine-containing compound metabolic process |
| A | 1901135 | biological_process | carbohydrate derivative metabolic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE CMU A1481 |
| Chain | Residue |
| A | HIS116 |
| A | ILE214 |
| A | SER217 |
| A | LYS221 |
| A | HOH2074 |
| A | SER117 |
| A | THR118 |
| A | ARG146 |
| A | LEU148 |
| A | THR151 |
| A | GLY152 |
| A | TYR199 |
| A | ARG202 |
Functional Information from PROSITE/UniProt
| site_id | PS00647 |
| Number of Residues | 16 |
| Details | THYMID_PHOSPHORYLASE Thymidine and pyrimidine-nucleoside phosphorylases signature. SGRGLghTGGTlDkLE |
| Chain | Residue | Details |
| A | SER144-GLU159 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 27 |
| Details | Repeat: {"description":"R-V-A-A-A-L-X(5,6)-L-G-R"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 16 |
| Details | Repeat: {"description":"R-A-L-X-X-A-L-V-L"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | Binding site: {} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1azy |
| Chain | Residue | Details |
| A | LYS221 | |
| A | HIS116 | |
| A | ARG202 |
| site_id | CSA2 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1azy |
| Chain | Residue | Details |
| A | LYS221 | |
| A | HIS116 | |
| A | SER217 | |
| A | ARG202 |
