3K4G
Crystal structure of E. coli RNA polymerase alpha subunit C-terminal domain
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003677 | molecular_function | DNA binding |
| A | 0003899 | molecular_function | DNA-directed 5'-3' RNA polymerase activity |
| A | 0006351 | biological_process | DNA-templated transcription |
| B | 0003677 | molecular_function | DNA binding |
| B | 0003899 | molecular_function | DNA-directed 5'-3' RNA polymerase activity |
| B | 0006351 | biological_process | DNA-templated transcription |
| C | 0003677 | molecular_function | DNA binding |
| C | 0003899 | molecular_function | DNA-directed 5'-3' RNA polymerase activity |
| C | 0006351 | biological_process | DNA-templated transcription |
| D | 0003677 | molecular_function | DNA binding |
| D | 0003899 | molecular_function | DNA-directed 5'-3' RNA polymerase activity |
| D | 0006351 | biological_process | DNA-templated transcription |
| E | 0003677 | molecular_function | DNA binding |
| E | 0003899 | molecular_function | DNA-directed 5'-3' RNA polymerase activity |
| E | 0006351 | biological_process | DNA-templated transcription |
| F | 0003677 | molecular_function | DNA binding |
| F | 0003899 | molecular_function | DNA-directed 5'-3' RNA polymerase activity |
| F | 0006351 | biological_process | DNA-templated transcription |
| G | 0003677 | molecular_function | DNA binding |
| G | 0003899 | molecular_function | DNA-directed 5'-3' RNA polymerase activity |
| G | 0006351 | biological_process | DNA-templated transcription |
| H | 0003677 | molecular_function | DNA binding |
| H | 0003899 | molecular_function | DNA-directed 5'-3' RNA polymerase activity |
| H | 0006351 | biological_process | DNA-templated transcription |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE NA A 2 |
| Chain | Residue |
| A | ASN320 |
| A | PRO322 |
| B | ASN320 |
| B | PRO322 |
| C | HOH107 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE NA C 4 |
| Chain | Residue |
| D | PRO322 |
| B | HOH204 |
| C | ASN320 |
| C | PRO322 |
| D | ASN320 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE NA E 3 |
| Chain | Residue |
| E | ASN320 |
| E | PRO322 |
| F | ASN320 |
| F | PRO322 |
| G | HOH331 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE NA G 1 |
| Chain | Residue |
| G | ASN320 |
| G | PRO322 |
| H | ASN320 |
| H | PRO322 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 8 |
| Details | MOD_RES: ADP-ribosylarginine => ECO:0000269|PubMed:4371081 |
| Chain | Residue | Details |
| A | ARG265 | |
| B | ARG265 | |
| C | ARG265 | |
| D | ARG265 | |
| E | ARG265 | |
| F | ARG265 | |
| G | ARG265 | |
| H | ARG265 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 8 |
| Details | MOD_RES: N6-acetyllysine => ECO:0000269|PubMed:21696463 |
| Chain | Residue | Details |
| A | MLY297 | |
| B | MLY297 | |
| C | MLY297 | |
| D | MLY297 | |
| E | MLY297 | |
| F | MLY297 | |
| G | MLY297 | |
| H | MLY297 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 8 |
| Details | MOD_RES: N6-acetyllysine; by PatZ => ECO:0000269|PubMed:21696463 |
| Chain | Residue | Details |
| A | MLY298 | |
| B | MLY298 | |
| C | MLY298 | |
| D | MLY298 | |
| E | MLY298 | |
| F | MLY298 | |
| G | MLY298 | |
| H | MLY298 |
