4E7X
Structural Basis for the Activity of a Cytoplasmic RNA Terminal U-transferase
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000287 | molecular_function | magnesium ion binding |
| A | 0002134 | molecular_function | UTP binding |
| A | 0003723 | molecular_function | RNA binding |
| A | 0005524 | molecular_function | ATP binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0016779 | molecular_function | nucleotidyltransferase activity |
| A | 0036450 | biological_process | polyuridylation-dependent decapping of nuclear-transcribed mRNA |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0050265 | molecular_function | RNA uridylyltransferase activity |
| A | 0071076 | biological_process | RNA 3' uridylation |
| A | 1990817 | molecular_function | poly(A) RNA polymerase activity |
| B | 0000287 | molecular_function | magnesium ion binding |
| B | 0002134 | molecular_function | UTP binding |
| B | 0003723 | molecular_function | RNA binding |
| B | 0005524 | molecular_function | ATP binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005829 | cellular_component | cytosol |
| B | 0016779 | molecular_function | nucleotidyltransferase activity |
| B | 0036450 | biological_process | polyuridylation-dependent decapping of nuclear-transcribed mRNA |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0050265 | molecular_function | RNA uridylyltransferase activity |
| B | 0071076 | biological_process | RNA 3' uridylation |
| B | 1990817 | molecular_function | poly(A) RNA polymerase activity |
| C | 0000287 | molecular_function | magnesium ion binding |
| C | 0002134 | molecular_function | UTP binding |
| C | 0003723 | molecular_function | RNA binding |
| C | 0005524 | molecular_function | ATP binding |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0005829 | cellular_component | cytosol |
| C | 0016779 | molecular_function | nucleotidyltransferase activity |
| C | 0036450 | biological_process | polyuridylation-dependent decapping of nuclear-transcribed mRNA |
| C | 0046872 | molecular_function | metal ion binding |
| C | 0050265 | molecular_function | RNA uridylyltransferase activity |
| C | 0071076 | biological_process | RNA 3' uridylation |
| C | 1990817 | molecular_function | poly(A) RNA polymerase activity |
| D | 0000287 | molecular_function | magnesium ion binding |
| D | 0002134 | molecular_function | UTP binding |
| D | 0003723 | molecular_function | RNA binding |
| D | 0005524 | molecular_function | ATP binding |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0005829 | cellular_component | cytosol |
| D | 0016779 | molecular_function | nucleotidyltransferase activity |
| D | 0036450 | biological_process | polyuridylation-dependent decapping of nuclear-transcribed mRNA |
| D | 0046872 | molecular_function | metal ion binding |
| D | 0050265 | molecular_function | RNA uridylyltransferase activity |
| D | 0071076 | biological_process | RNA 3' uridylation |
| D | 1990817 | molecular_function | poly(A) RNA polymerase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE ACT A 501 |
| Chain | Residue |
| A | TYR279 |
| A | PHE283 |
| A | ARG351 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ACT B 501 |
| Chain | Residue |
| B | TYR279 |
| B | PHE283 |
| B | PRO285 |
| B | ARG351 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE ACT C 501 |
| Chain | Residue |
| C | ARG351 |
| C | TYR279 |
| C | PHE283 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE ACT D 501 |
| Chain | Residue |
| D | TYR279 |
| D | PHE283 |
| D | ARG351 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:22608966, ECO:0000269|PubMed:22751018, ECO:0000269|PubMed:22885303, ECO:0000269|PubMed:24322298, ECO:0007744|PDB:4E80, ECO:0007744|PDB:4EP7, ECO:0007744|PDB:4FH5, ECO:0007744|PDB:4FHP, ECO:0007744|PDB:4FHW, ECO:0007744|PDB:4FHX, ECO:0007744|PDB:4NKT |
| Chain | Residue | Details |
| A | SER90 | |
| B | SER90 | |
| C | SER90 | |
| D | SER90 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:22608966, ECO:0000269|PubMed:22885303, ECO:0007744|PDB:4EP7, ECO:0007744|PDB:4FH5, ECO:0007744|PDB:4FHP, ECO:0007744|PDB:4FHW, ECO:0007744|PDB:4FHX, ECO:0007744|PDB:4FHY |
| Chain | Residue | Details |
| B | ASP101 | |
| C | ASP101 | |
| D | ASP101 | |
| A | ASP101 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:22608966, ECO:0000269|PubMed:22885303, ECO:0007744|PDB:4EP7, ECO:0007744|PDB:4FH5, ECO:0007744|PDB:4FHP, ECO:0007744|PDB:4FHV, ECO:0007744|PDB:4FHW, ECO:0007744|PDB:4FHX, ECO:0007744|PDB:4FHY |
| Chain | Residue | Details |
| A | ASP103 | |
| B | ASP103 | |
| C | ASP103 | |
| D | ASP103 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:22885303, ECO:0007744|PDB:4FHP, ECO:0007744|PDB:4FHW |
| Chain | Residue | Details |
| A | ALA168 | |
| B | ALA168 | |
| C | ALA168 | |
| D | ALA168 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:22608966, ECO:0000269|PubMed:22751018, ECO:0000269|PubMed:22885303, ECO:0000269|PubMed:24322298, ECO:0007744|PDB:4E80, ECO:0007744|PDB:4EP7, ECO:0007744|PDB:4FH5, ECO:0007744|PDB:4FHP, ECO:0007744|PDB:4FHV, ECO:0007744|PDB:4FHX, ECO:0007744|PDB:4NKT, ECO:0007744|PDB:4NKU |
| Chain | Residue | Details |
| A | ASN171 | |
| B | ASN171 | |
| C | ASN171 | |
| D | ASN171 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:22608966, ECO:0000269|PubMed:22885303, ECO:0000269|PubMed:24322298, ECO:0007744|PDB:4EP7, ECO:0007744|PDB:4FHP, ECO:0007744|PDB:4NKT, ECO:0007744|PDB:4NKU |
| Chain | Residue | Details |
| A | THR172 | |
| B | THR172 | |
| C | THR172 | |
| D | THR172 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 8 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:22608966, ECO:0000269|PubMed:22751018, ECO:0000269|PubMed:22885303, ECO:0000269|PubMed:24322298, ECO:0007744|PDB:4E80, ECO:0007744|PDB:4EP7, ECO:0007744|PDB:4FH5, ECO:0007744|PDB:4FHP, ECO:0007744|PDB:4FHV, ECO:0007744|PDB:4FHW, ECO:0007744|PDB:4FHX, ECO:0007744|PDB:4NKT |
| Chain | Residue | Details |
| A | LYS193 | |
| A | SER211 | |
| B | LYS193 | |
| B | SER211 | |
| C | LYS193 | |
| C | SER211 | |
| D | LYS193 | |
| D | SER211 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:22608966, ECO:0000269|PubMed:22751018, ECO:0000269|PubMed:22885303, ECO:0000269|PubMed:24322298, ECO:0007744|PDB:4E80, ECO:0007744|PDB:4EP7, ECO:0007744|PDB:4FH5, ECO:0007744|PDB:4FHP, ECO:0007744|PDB:4FHV, ECO:0007744|PDB:4FHW, ECO:0007744|PDB:4NKT |
| Chain | Residue | Details |
| A | LYS197 | |
| B | LYS197 | |
| C | LYS197 | |
| D | LYS197 |
| site_id | SWS_FT_FI9 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:22608966, ECO:0000269|PubMed:22751018, ECO:0000269|PubMed:22885303, ECO:0000269|PubMed:24322298, ECO:0007744|PDB:4E80, ECO:0007744|PDB:4EP7, ECO:0007744|PDB:4FH5, ECO:0007744|PDB:4FHP, ECO:0007744|PDB:4FHV, ECO:0007744|PDB:4FHW, ECO:0007744|PDB:4NKT, ECO:0007744|PDB:4NKU |
| Chain | Residue | Details |
| A | TYR212 | |
| B | TYR212 | |
| C | TYR212 | |
| D | TYR212 |
| site_id | SWS_FT_FI10 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:22608966, ECO:0000269|PubMed:22885303, ECO:0000269|PubMed:24322298, ECO:0007744|PDB:4EP7, ECO:0007744|PDB:4FH5, ECO:0007744|PDB:4FHP, ECO:0007744|PDB:4FHV, ECO:0007744|PDB:4FHW, ECO:0007744|PDB:4NKT, ECO:0007744|PDB:4NKU |
| Chain | Residue | Details |
| A | HIS336 | |
| B | HIS336 | |
| C | HIS336 | |
| D | HIS336 |
| site_id | SWS_FT_FI11 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:22885303, ECO:0007744|PDB:4FHX |
| Chain | Residue | Details |
| A | ARG340 | |
| B | ARG340 | |
| C | ARG340 | |
| D | ARG340 |
