8QHQ
Crystal structure of human DNPH1 bound to hmdUMP
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0009159 | biological_process | deoxyribonucleoside monophosphate catabolic process |
| A | 0070694 | molecular_function | deoxyribonucleoside 5'-monophosphate N-glycosidase activity |
| B | 0009159 | biological_process | deoxyribonucleoside monophosphate catabolic process |
| B | 0070694 | molecular_function | deoxyribonucleoside 5'-monophosphate N-glycosidase activity |
| C | 0009159 | biological_process | deoxyribonucleoside monophosphate catabolic process |
| C | 0070694 | molecular_function | deoxyribonucleoside 5'-monophosphate N-glycosidase activity |
| D | 0009159 | biological_process | deoxyribonucleoside monophosphate catabolic process |
| D | 0070694 | molecular_function | deoxyribonucleoside 5'-monophosphate N-glycosidase activity |
| E | 0009159 | biological_process | deoxyribonucleoside monophosphate catabolic process |
| E | 0070694 | molecular_function | deoxyribonucleoside 5'-monophosphate N-glycosidase activity |
| F | 0009159 | biological_process | deoxyribonucleoside monophosphate catabolic process |
| F | 0070694 | molecular_function | deoxyribonucleoside 5'-monophosphate N-glycosidase activity |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 42 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:25108359, ECO:0007744|PDB:4P5E |
| Chain | Residue | Details |
| A | GLY27 | |
| B | ARG30 | |
| B | GLY31 | |
| B | SER98 | |
| B | GLY100 | |
| B | GLN104 | |
| C | GLY27 | |
| C | ILE29 | |
| C | ARG30 | |
| C | GLY31 | |
| C | SER98 | |
| A | ILE29 | |
| C | GLY100 | |
| C | GLN104 | |
| D | GLY27 | |
| D | ILE29 | |
| D | ARG30 | |
| D | GLY31 | |
| D | SER98 | |
| D | GLY100 | |
| D | GLN104 | |
| E | GLY27 | |
| A | ARG30 | |
| E | ILE29 | |
| E | ARG30 | |
| E | GLY31 | |
| E | SER98 | |
| E | GLY100 | |
| E | GLN104 | |
| F | GLY27 | |
| F | ILE29 | |
| F | ARG30 | |
| F | GLY31 | |
| A | GLY31 | |
| F | SER98 | |
| F | GLY100 | |
| F | GLN104 | |
| A | SER98 | |
| A | GLY100 | |
| A | GLN104 | |
| B | GLY27 | |
| B | ILE29 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 6 |
| Details | BINDING: in other chain => ECO:0000269|PubMed:25108359, ECO:0007744|PDB:4P5E |
| Chain | Residue | Details |
| A | SER128 | |
| B | SER128 | |
| C | SER128 | |
| D | SER128 | |
| E | SER128 | |
| F | SER128 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 6 |
| Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163 |
| Chain | Residue | Details |
| A | SER28 | |
| B | SER28 | |
| C | SER28 | |
| D | SER28 | |
| E | SER28 | |
| F | SER28 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 18 |
| Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:24275569 |
| Chain | Residue | Details |
| A | SER98 | |
| D | SER98 | |
| D | SER128 | |
| D | SER138 | |
| E | SER98 | |
| E | SER128 | |
| E | SER138 | |
| F | SER98 | |
| F | SER128 | |
| F | SER138 | |
| A | SER128 | |
| A | SER138 | |
| B | SER98 | |
| B | SER128 | |
| B | SER138 | |
| C | SER98 | |
| C | SER128 | |
| C | SER138 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 6 |
| Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163 |
| Chain | Residue | Details |
| A | SER123 | |
| B | SER123 | |
| C | SER123 | |
| D | SER123 | |
| E | SER123 | |
| F | SER123 |
