4NHM
Crystal structure of Tpa1p from Saccharomyces cerevisiae, termination and polyadenylation protein 1, in complex with N-[(1-chloro-4-hydroxyisoquinolin-3-yl)carbonyl]glycine (IOX3/UN9)
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000288 | biological_process | nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay |
| A | 0005506 | molecular_function | iron ion binding |
| A | 0005634 | cellular_component | nucleus |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0006415 | biological_process | translational termination |
| A | 0006449 | biological_process | regulation of translational termination |
| A | 0006450 | biological_process | regulation of translational fidelity |
| A | 0008143 | molecular_function | poly(A) binding |
| A | 0008198 | molecular_function | ferrous iron binding |
| A | 0009896 | biological_process | positive regulation of catabolic process |
| A | 0010604 | biological_process | positive regulation of macromolecule metabolic process |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0016705 | molecular_function | oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen |
| A | 0016706 | molecular_function | 2-oxoglutarate-dependent dioxygenase activity |
| A | 0018188 | biological_process | peptidyl-proline di-hydroxylation |
| A | 0031418 | molecular_function | L-ascorbic acid binding |
| A | 0031543 | molecular_function | peptidyl-proline dioxygenase activity |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0051213 | molecular_function | dioxygenase activity |
| A | 0051246 | biological_process | regulation of protein metabolic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE UN9 A 701 |
| Chain | Residue |
| A | ASN148 |
| A | VAL229 |
| A | ARG238 |
| A | GLN242 |
| A | TRP244 |
| A | MN702 |
| A | GOL703 |
| A | HOH814 |
| A | HOH1325 |
| A | HOH1329 |
| A | TYR150 |
| A | LEU156 |
| A | HIS159 |
| A | ASP161 |
| A | ILE171 |
| A | TYR173 |
| A | LEU189 |
| A | HIS227 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MN A 702 |
| Chain | Residue |
| A | HIS159 |
| A | ASP161 |
| A | HIS227 |
| A | UN9701 |
| A | HOH1325 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL A 703 |
| Chain | Residue |
| A | ILE87 |
| A | LEU156 |
| A | UN9701 |
| A | HOH960 |
| A | HOH1204 |
| A | HOH1329 |
| site_id | AC4 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL A 704 |
| Chain | Residue |
| A | PHE519 |
| A | ASN520 |
| A | LEU523 |
| A | LYS524 |
| A | ILE529 |
| A | ILE530 |
| A | ASP531 |
| A | ASP631 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 106 |
| Details | Domain: {"description":"Fe2OG dioxygenase","evidences":[{"source":"PROSITE-ProRule","id":"PRU00805","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 3 |
| Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00805","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"20040577","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"25728928","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"20040577","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00805","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"20040577","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"18407956","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
