4NHK
Crystal structure of Tpa1p from Saccharomyces cerevisiae, termination and polyadenylation protein 1, in complex with pyridine-2,4-dicarboxylic acid (2,4-PDCA)
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 | 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 |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MN A 701 |
Chain | Residue |
A | HIS159 |
A | ASP161 |
A | HIS227 |
A | PD2702 |
A | HOH801 |
site_id | AC2 |
Number of Residues | 18 |
Details | BINDING SITE FOR RESIDUE PD2 A 702 |
Chain | Residue |
A | HIS227 |
A | VAL229 |
A | SER240 |
A | GLN242 |
A | TRP244 |
A | MN701 |
A | GOL703 |
A | GOL704 |
A | HOH801 |
A | HOH812 |
A | HOH857 |
A | HOH922 |
A | HOH993 |
A | HOH1158 |
A | LEU156 |
A | HIS159 |
A | ASP161 |
A | ILE171 |
site_id | AC3 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE GOL A 703 |
Chain | Residue |
A | TYR88 |
A | GLN92 |
A | ASN148 |
A | PD2702 |
A | HOH812 |
site_id | AC4 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE GOL A 704 |
Chain | Residue |
A | HIS159 |
A | ASP161 |
A | ARG166 |
A | PD2702 |
A | HOH975 |
A | HOH993 |
site_id | AC5 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE GOL A 705 |
Chain | Residue |
A | TYR422 |
A | ARG423 |
A | ASN424 |
A | HOH839 |
A | HOH1004 |
site_id | AC6 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE GOL A 706 |
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 | 3 |
Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00805, ECO:0000269|PubMed:20040577, ECO:0000269|PubMed:25728928 |
Chain | Residue | Details |
A | HIS159 | |
A | ASP161 | |
A | HIS227 |
site_id | SWS_FT_FI2 |
Number of Residues | 1 |
Details | BINDING: BINDING => ECO:0000269|PubMed:20040577 |
Chain | Residue | Details |
A | TYR173 |
site_id | SWS_FT_FI3 |
Number of Residues | 1 |
Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00805, ECO:0000269|PubMed:20040577 |
Chain | Residue | Details |
A | ARG238 |
site_id | SWS_FT_FI4 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:18407956 |
Chain | Residue | Details |
A | SER607 |