2XJE
Crystal structure of the D52N variant of cytosolic 5'-nucleotidase II in complex with uridine 5'-monophosphate and adenosine triphosphate
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0000255 | biological_process | allantoin metabolic process |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005524 | molecular_function | ATP binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0006204 | biological_process | IMP catabolic process |
| A | 0008253 | molecular_function | 5'-nucleotidase activity |
| A | 0009117 | biological_process | nucleotide metabolic process |
| A | 0016740 | molecular_function | transferase activity |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0046037 | biological_process | GMP metabolic process |
| A | 0046040 | biological_process | IMP metabolic process |
| A | 0046054 | biological_process | dGMP metabolic process |
| A | 0046055 | biological_process | dGMP catabolic process |
| A | 0046085 | biological_process | adenosine metabolic process |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0050146 | molecular_function | nucleoside phosphotransferase activity |
| A | 0050689 | biological_process | negative regulation of defense response to virus by host |
| A | 0061630 | molecular_function | ubiquitin protein ligase activity |
| A | 0070936 | biological_process | protein K48-linked ubiquitination |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE U5P A 1489 |
| Chain | Residue |
| A | ASN52 |
| A | LYS215 |
| A | THR249 |
| A | ASN250 |
| A | SER251 |
| A | LYS292 |
| A | MG1493 |
| A | HOH2138 |
| A | HOH2140 |
| A | HOH2172 |
| A | HOH2173 |
| A | MET53 |
| A | HOH2174 |
| A | ASP54 |
| A | PHE157 |
| A | ARG202 |
| A | VAL205 |
| A | ASP206 |
| A | HIS209 |
| A | TYR210 |
| site_id | AC2 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE ATP A 1490 |
| Chain | Residue |
| A | ARG144 |
| A | ASP145 |
| A | THR147 |
| A | ASN154 |
| A | PHE354 |
| A | LYS362 |
| A | GLN453 |
| A | ARG456 |
| A | ARG456 |
| A | TYR457 |
| A | MG1492 |
| A | MG1492 |
| A | HOH2175 |
| A | HOH2175 |
| A | HOH2177 |
| site_id | AC3 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL A 1491 |
| Chain | Residue |
| A | GLN280 |
| A | PHE283 |
| A | ASP284 |
| A | ILE286 |
| A | GLN322 |
| A | HIS323 |
| A | GLY324 |
| A | ILE325 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG A 1492 |
| Chain | Residue |
| A | ATP1490 |
| A | ATP1490 |
| A | HOH2175 |
| A | HOH2175 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG A 1493 |
| Chain | Residue |
| A | ASN52 |
| A | ASP54 |
| A | ASP351 |
| A | U5P1489 |
| A | HOH2138 |
| A | HOH2140 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Nucleophile","evidences":[{"source":"PubMed","id":"21396942","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Proton donor","evidences":[{"source":"PubMed","id":"21396942","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"17405878","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"21396942","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2J2C","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2JC9","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2JCM","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2XCV","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2XCW","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2XJB","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2XJC","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2XJD","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2XJE","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"21396942","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2XJB","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"21396942","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2XJC","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 7 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"21396942","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2XCV","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2XCW","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 1 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"17405878","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"21396942","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2J2C","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2JC9","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2JCM","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 1 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"17405878","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2JC9","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
