3ERC
Crystal structure of the heterodimeric vaccinia virus mRNA polyadenylate polymerase with three fragments of RNA and 3'-deoxy ATP
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003746 | molecular_function | translation elongation factor activity |
| A | 0004483 | molecular_function | mRNA (nucleoside-2'-O-)-methyltransferase activity |
| A | 0006370 | biological_process | 7-methylguanosine mRNA capping |
| A | 0031440 | biological_process | regulation of mRNA 3'-end processing |
| B | 0003746 | molecular_function | translation elongation factor activity |
| B | 0004483 | molecular_function | mRNA (nucleoside-2'-O-)-methyltransferase activity |
| B | 0006370 | biological_process | 7-methylguanosine mRNA capping |
| B | 0031440 | biological_process | regulation of mRNA 3'-end processing |
| C | 0005524 | molecular_function | ATP binding |
| C | 0006397 | biological_process | mRNA processing |
| C | 0016740 | molecular_function | transferase activity |
| C | 0046872 | molecular_function | metal ion binding |
| C | 1990817 | molecular_function | poly(A) RNA polymerase activity |
| D | 0005524 | molecular_function | ATP binding |
| D | 0006397 | biological_process | mRNA processing |
| D | 0016740 | molecular_function | transferase activity |
| D | 0046872 | molecular_function | metal ion binding |
| D | 1990817 | molecular_function | poly(A) RNA polymerase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE U C 600 |
| Chain | Residue |
| C | ASN90 |
| C | LYS93 |
| C | THR96 |
| C | ASP475 |
| C | ILE476 |
| C | ILE477 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE U D 602 |
| Chain | Residue |
| D | ASP475 |
| D | ILE476 |
| D | ILE477 |
| D | ASN90 |
| D | LYS93 |
| D | THR96 |
| site_id | AC3 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE 3AT D 800 |
| Chain | Residue |
| D | GLY187 |
| D | SER188 |
| D | GLY201 |
| D | ASP202 |
| D | ASP204 |
| D | ASN284 |
| D | MET288 |
| D | ARG294 |
| D | LYS304 |
| D | ARG308 |
| D | ASN402 |
| D | CA904 |
| E | DC605 |
| site_id | AC4 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE 3AT C 801 |
| Chain | Residue |
| C | GLY187 |
| C | SER188 |
| C | GLY201 |
| C | ASP202 |
| C | ASP204 |
| C | ASN284 |
| C | MET288 |
| C | ARG294 |
| C | LYS304 |
| C | ARG308 |
| C | ASN402 |
| C | CA902 |
| F | DC610 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CA C 901 |
| Chain | Residue |
| C | ASP202 |
| C | ASP204 |
| C | ASP253 |
| F | DC610 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CA C 902 |
| Chain | Residue |
| C | ASP202 |
| C | ASP204 |
| C | 3AT801 |
| F | DC610 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CA D 903 |
| Chain | Residue |
| D | ASP202 |
| D | ASP204 |
| D | ASP253 |
| E | DC605 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CA D 904 |
| Chain | Residue |
| D | ASP202 |
| D | ASP204 |
| D | 3AT800 |
| E | DC605 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | ACT_SITE: ACT_SITE => ECO:0000255|PIRSR:PIRSR015693-50 |
| Chain | Residue | Details |
| C | ASP202 | |
| C | ASP204 | |
| D | ASP202 | |
| D | ASP204 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 6 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:16678106, ECO:0000269|PubMed:19446524, ECO:0007744|PDB:3ERC |
| Chain | Residue | Details |
| C | ASP202 | |
| B | GLU233 | |
| C | ASP204 | |
| C | ASP253 | |
| D | ASP202 | |
| D | ASP204 | |
| D | ASP253 | |
| B | ARG177 | |
| B | ASP182 | |
| B | SER205 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 16 |
| Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00944, ECO:0000269|PubMed:8612277 |
| Chain | Residue | Details |
| A | GLN39 | |
| B | TYR66 | |
| B | GLY68 | |
| B | GLY72 | |
| B | ASP95 | |
| B | ARG97 | |
| B | VAL116 | |
| B | ASP138 | |
| A | TYR66 | |
| A | GLY68 | |
| A | GLY72 | |
| A | ASP95 | |
| A | ARG97 | |
| A | VAL116 | |
| A | ASP138 | |
| B | GLN39 |
