4KG4
Crystal structure of Saccharomyces cerevisiae Dcp2 Nudix domain (E198Q mutation)
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000184 | biological_process | nuclear-transcribed mRNA catabolic process, nonsense-mediated decay |
| A | 0000290 | biological_process | deadenylation-dependent decapping of nuclear-transcribed mRNA |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0140933 | molecular_function | 5'-(N(7)-methylguanosine 5'-triphospho)-[mRNA] hydrolase activity |
| B | 0000184 | biological_process | nuclear-transcribed mRNA catabolic process, nonsense-mediated decay |
| B | 0000290 | biological_process | deadenylation-dependent decapping of nuclear-transcribed mRNA |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0140933 | molecular_function | 5'-(N(7)-methylguanosine 5'-triphospho)-[mRNA] hydrolase activity |
Functional Information from PROSITE/UniProt
| site_id | PS00893 |
| Number of Residues | 22 |
| Details | NUDIX_BOX Nudix box signature. GkiskdEndidCCiREVkEEiG |
| Chain | Residue | Details |
| A | GLY134-GLY155 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 42 |
| Details | Motif: {"description":"Nudix box"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"18407956","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 127 |
| Details | Domain: {"description":"Nudix hydrolase","evidences":[{"source":"PROSITE-ProRule","id":"PRU00794","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
