1SZ3
CRYSTAL STRUCTURE OF NUDIX HYDROLASE DR1025 IN COMPLEXED WITH GNP AND MG+2
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 |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0005524 | molecular_function | ATP binding |
| B | 0008413 | molecular_function | 8-oxo-7,8-dihydroguanosine triphosphate pyrophosphatase activity |
| B | 0008828 | molecular_function | dATP diphosphatase activity |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0019177 | molecular_function | dihydroneopterin triphosphate pyrophosphohydrolase activity |
| B | 0046654 | biological_process | tetrahydrofolate biosynthetic process |
| B | 0046656 | biological_process | folic acid biosynthetic process |
| B | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG A 201 |
| Chain | Residue |
| A | GLU65 |
| A | HOH765 |
| A | HOH846 |
| A | HOH853 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG B 202 |
| Chain | Residue |
| B | GLU65 |
| B | HOH817 |
| B | HOH844 |
| B | HOH878 |
| site_id | AC3 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE GNP A 3030 |
| Chain | Residue |
| A | ALA15 |
| A | HIS46 |
| A | SER49 |
| A | GLY50 |
| A | ALA51 |
| A | GLU69 |
| A | PHE87 |
| A | ASP89 |
| A | ILE93 |
| A | ARG95 |
| A | HOH810 |
| A | HOH845 |
| B | MET1 |
| B | GLU2 |
| B | ASP4 |
| B | ARG6 |
| A | LEU13 |
| site_id | AC4 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE GNP A 2030 |
| Chain | Residue |
| A | MET1 |
| A | GLU2 |
| A | ASP4 |
| A | HOH793 |
| A | HOH804 |
| A | HOH862 |
| B | LEU13 |
| B | ALA15 |
| B | SER49 |
| B | GLY50 |
| B | ALA51 |
| B | PHE87 |
| B | PRO88 |
| B | ASP89 |
| B | VAL91 |
| B | ILE93 |
| B | ARG95 |
| B | HOH817 |
| B | HOH867 |
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 | 42 |
| 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 | 18 |
| 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 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 10 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"15123424","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1SU2","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
