1SJY
Crystal Structure of NUDIX HYDROLASE DR1025 FROM DEINOCOCCUS RADIODURANS
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0005524 | molecular_function | ATP binding |
| A | 0008413 | molecular_function | 8-oxo-7,8-dihydroguanosine triphosphate pyrophosphatase activity |
| A | 0008828 | molecular_function | dATP diphosphatase activity |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0019177 | molecular_function | dihydroneopterin triphosphate pyrophosphohydrolase activity |
| A | 0046654 | biological_process | tetrahydrofolate biosynthetic process |
| A | 0046656 | biological_process | folic acid biosynthetic process |
| A | 0046872 | molecular_function | metal ion binding |
Functional Information from PROSITE/UniProt
| site_id | PS00893 |
| Number of Residues | 22 |
| Details | NUDIX_BOX Nudix box signature. GavedgEnpqdAAvREAcEEtG |
| Chain | Residue | Details |
| A | GLY50-GLY71 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 21 |
| Details | Motif: {"description":"Nudix box","evidences":[{"source":"PROSITE-ProRule","id":"PRU00794","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"15123424","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"15123424","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1SU2","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"15123424","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1SU2","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1SZ3","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
