5OF3
Crystal structure of the heterotrimeric PriSLX primase from S. solfataricus.
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000428 | cellular_component | DNA-directed RNA polymerase complex |
| A | 0003899 | molecular_function | DNA-directed RNA polymerase activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0006259 | biological_process | DNA metabolic process |
| A | 0006260 | biological_process | DNA replication |
| A | 0006269 | biological_process | DNA replication, synthesis of primer |
| A | 0016740 | molecular_function | transferase activity |
| A | 0016779 | molecular_function | nucleotidyltransferase activity |
| A | 0046872 | molecular_function | metal ion binding |
| A | 1990077 | cellular_component | primosome complex |
| B | 0003899 | molecular_function | DNA-directed RNA polymerase activity |
| B | 0005515 | molecular_function | protein binding |
| B | 0006260 | biological_process | DNA replication |
| B | 0006269 | biological_process | DNA replication, synthesis of primer |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0051536 | molecular_function | iron-sulfur cluster binding |
| B | 0051539 | molecular_function | 4 iron, 4 sulfur cluster binding |
| B | 1990077 | cellular_component | primosome complex |
| C | 0046872 | molecular_function | metal ion binding |
| D | 0000428 | cellular_component | DNA-directed RNA polymerase complex |
| D | 0003899 | molecular_function | DNA-directed RNA polymerase activity |
| D | 0005515 | molecular_function | protein binding |
| D | 0006259 | biological_process | DNA metabolic process |
| D | 0006260 | biological_process | DNA replication |
| D | 0006269 | biological_process | DNA replication, synthesis of primer |
| D | 0016740 | molecular_function | transferase activity |
| D | 0016779 | molecular_function | nucleotidyltransferase activity |
| D | 0046872 | molecular_function | metal ion binding |
| D | 1990077 | cellular_component | primosome complex |
| E | 0003899 | molecular_function | DNA-directed RNA polymerase activity |
| E | 0005515 | molecular_function | protein binding |
| E | 0006260 | biological_process | DNA replication |
| E | 0006269 | biological_process | DNA replication, synthesis of primer |
| E | 0046872 | molecular_function | metal ion binding |
| E | 0051536 | molecular_function | iron-sulfur cluster binding |
| E | 0051539 | molecular_function | 4 iron, 4 sulfur cluster binding |
| E | 1990077 | cellular_component | primosome complex |
| F | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 14 |
| Details | binding site for residue APC A 1001 |
| Chain | Residue |
| A | TYR48 |
| A | ARG244 |
| A | LEU245 |
| A | ARG247 |
| A | HIS253 |
| A | MN1002 |
| A | PHE74 |
| A | ASP101 |
| A | ASP103 |
| A | SER173 |
| A | ASN175 |
| A | ARG176 |
| A | HIS179 |
| A | VAL238 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | binding site for residue MN A 1002 |
| Chain | Residue |
| A | ASP101 |
| A | ASP103 |
| A | APC1001 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | binding site for residue ZN A 1003 |
| Chain | Residue |
| A | CYS116 |
| A | CYS119 |
| A | CYS128 |
| A | ASP131 |
| site_id | AC4 |
| Number of Residues | 14 |
| Details | binding site for residue APC D 1001 |
| Chain | Residue |
| A | ARG67 |
| D | TYR48 |
| D | PHE74 |
| D | ASP101 |
| D | ASP103 |
| D | SER173 |
| D | ASN175 |
| D | ARG176 |
| D | HIS179 |
| D | ARG244 |
| D | LEU245 |
| D | ARG247 |
| D | HIS253 |
| D | MN1002 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | binding site for residue MN D 1002 |
| Chain | Residue |
| D | ASP101 |
| D | ASP103 |
| D | APC1001 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | binding site for residue ZN D 1003 |
| Chain | Residue |
| D | CYS116 |
| D | CYS119 |
| D | CYS128 |
| D | ASP131 |
| site_id | AC7 |
| Number of Residues | 12 |
| Details | binding site for residue APC C 1001 |
| Chain | Residue |
| A | GLU89 |
| A | GLU90 |
| C | GLN69 |
| C | ASP70 |
| C | SER71 |
| C | ARG72 |
| C | LYS73 |
| C | ARG74 |
| C | LEU77 |
| C | TYR103 |
| C | TRP115 |
| C | MN1002 |
| site_id | AC8 |
| Number of Residues | 2 |
| Details | binding site for residue MN C 1002 |
| Chain | Residue |
| C | ASP70 |
| C | APC1001 |
| site_id | AC9 |
| Number of Residues | 12 |
| Details | binding site for residue APC F 1001 |
| Chain | Residue |
| D | GLU89 |
| D | GLU90 |
| F | GLN69 |
| F | ASP70 |
| F | SER71 |
| F | ARG72 |
| F | LYS73 |
| F | ARG74 |
| F | LEU77 |
| F | TYR103 |
| F | TRP115 |
| F | MN1002 |
| site_id | AD1 |
| Number of Residues | 2 |
| Details | binding site for residue MN F 1002 |
| Chain | Residue |
| F | ASP70 |
| F | APC1001 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 6 |
| Details | Active site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00700","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"16273105","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 3 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00701","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
