3KT1
Crystal structure of Tpa1 from Saccharomyces cerevisiae, a component of the messenger ribonucleoprotein complex
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 | 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 |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE FE A 653 |
| Chain | Residue |
| A | HIS159 |
| A | ASP161 |
| A | HIS227 |
| A | HOH797 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 A 654 |
| Chain | Residue |
| A | ARG179 |
| A | LYS180 |
| A | LYS182 |
| site_id | AC3 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE SO4 A 655 |
| Chain | Residue |
| A | TRP546 |
| A | TRP546 |
| A | GLU547 |
| A | GLU547 |
| A | SER548 |
| A | SER548 |
| A | HOH764 |
| A | HOH764 |
| A | GLY545 |
| A | GLY545 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 A 656 |
| Chain | Residue |
| A | LYS152 |
| A | VAL234 |
| A | ASP235 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 A 657 |
| Chain | Residue |
| A | LYS180 |
| A | LYS182 |
| A | SER183 |
| A | HOH663 |
| A | HOH855 |
| site_id | AC6 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE GOL A 658 |
| Chain | Residue |
| A | GLN444 |
| A | LYS447 |
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 | HIS227 | |
| A | ASP161 |
| 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 |
