6R5D
Crystal structure of the Pri1 subunit of human primase bound to dATP
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000287 | molecular_function | magnesium ion binding |
| 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 | 0005654 | cellular_component | nucleoplasm |
| A | 0005658 | cellular_component | alpha DNA polymerase:primase complex |
| A | 0006260 | biological_process | DNA replication |
| A | 0006269 | biological_process | DNA replication, synthesis of primer |
| A | 0006270 | biological_process | DNA replication initiation |
| A | 0008270 | molecular_function | zinc ion binding |
| A | 0016020 | cellular_component | membrane |
| A | 0016740 | molecular_function | transferase activity |
| A | 0016779 | molecular_function | nucleotidyltransferase activity |
| A | 0032553 | molecular_function | ribonucleotide binding |
| A | 0046872 | molecular_function | metal ion binding |
| E | 0000287 | molecular_function | magnesium ion binding |
| E | 0000428 | cellular_component | DNA-directed RNA polymerase complex |
| E | 0003899 | molecular_function | DNA-directed RNA polymerase activity |
| E | 0005515 | molecular_function | protein binding |
| E | 0005654 | cellular_component | nucleoplasm |
| E | 0005658 | cellular_component | alpha DNA polymerase:primase complex |
| E | 0006260 | biological_process | DNA replication |
| E | 0006269 | biological_process | DNA replication, synthesis of primer |
| E | 0006270 | biological_process | DNA replication initiation |
| E | 0008270 | molecular_function | zinc ion binding |
| E | 0016020 | cellular_component | membrane |
| E | 0016740 | molecular_function | transferase activity |
| E | 0016779 | molecular_function | nucleotidyltransferase activity |
| E | 0032553 | molecular_function | ribonucleotide binding |
| E | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | binding site for residue ZN A 501 |
| Chain | Residue |
| A | CYS121 |
| A | CYS122 |
| A | CYS128 |
| A | CYS131 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | binding site for residue MN A 502 |
| Chain | Residue |
| A | ASP109 |
| A | ASP111 |
| A | MN503 |
| A | DTP504 |
| A | HOH650 |
| site_id | AC3 |
| Number of Residues | 7 |
| Details | binding site for residue MN A 503 |
| Chain | Residue |
| A | ASP109 |
| A | ASP111 |
| A | ASP306 |
| A | MN502 |
| A | DTP504 |
| A | HOH696 |
| A | HOH762 |
| site_id | AC4 |
| Number of Residues | 16 |
| Details | binding site for residue DTP A 504 |
| Chain | Residue |
| A | ASP109 |
| A | ASP111 |
| A | SER160 |
| A | ARG162 |
| A | ARG163 |
| A | HIS166 |
| A | HIS315 |
| A | LEU316 |
| A | LEU317 |
| A | LYS318 |
| A | HIS324 |
| A | MN502 |
| A | MN503 |
| A | HOH623 |
| A | HOH650 |
| A | HOH696 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | binding site for residue EDO A 505 |
| Chain | Residue |
| A | THR349 |
| A | SER351 |
| E | ASP149 |
| E | PHE150 |
| E | TYR188 |
| E | HOH648 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | binding site for residue EDO A 506 |
| Chain | Residue |
| A | ASP126 |
| A | ILE127 |
| A | EDO510 |
| A | HOH642 |
| E | SER173 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | binding site for residue EDO A 507 |
| Chain | Residue |
| A | LYS153 |
| A | HIS154 |
| A | ARG155 |
| A | ASN401 |
| A | HOH660 |
| site_id | AC8 |
| Number of Residues | 3 |
| Details | binding site for residue EDO A 508 |
| Chain | Residue |
| A | HOH630 |
| A | HOH637 |
| E | ARG355 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | binding site for residue EDO A 509 |
| Chain | Residue |
| A | ASN217 |
| A | LYS220 |
| A | TRP294 |
| E | ASP51 |
| site_id | AD1 |
| Number of Residues | 4 |
| Details | binding site for residue EDO A 510 |
| Chain | Residue |
| A | TYR159 |
| A | ARG329 |
| A | PRO344 |
| A | EDO506 |
| site_id | AD2 |
| Number of Residues | 2 |
| Details | binding site for residue EDO A 511 |
| Chain | Residue |
| A | ARG19 |
| A | ARG381 |
| site_id | AD3 |
| Number of Residues | 4 |
| Details | binding site for residue ZN E 501 |
| Chain | Residue |
| E | CYS121 |
| E | CYS122 |
| E | CYS128 |
| E | CYS131 |
| site_id | AD4 |
| Number of Residues | 5 |
| Details | binding site for residue MN E 502 |
| Chain | Residue |
| E | ASP109 |
| E | ASP111 |
| E | MN503 |
| E | DTP504 |
| E | HOH699 |
| site_id | AD5 |
| Number of Residues | 7 |
| Details | binding site for residue MN E 503 |
| Chain | Residue |
| E | ASP109 |
| E | ASP111 |
| E | ASP306 |
| E | MN502 |
| E | DTP504 |
| E | HOH675 |
| E | HOH688 |
| site_id | AD6 |
| Number of Residues | 19 |
| Details | binding site for residue DTP E 504 |
| Chain | Residue |
| A | ARG278 |
| E | TYR54 |
| E | ASP79 |
| E | ASP109 |
| E | ASP111 |
| E | SER160 |
| E | ARG162 |
| E | ARG163 |
| E | HIS166 |
| E | HIS315 |
| E | LEU316 |
| E | LEU317 |
| E | LYS318 |
| E | HIS324 |
| E | MN502 |
| E | MN503 |
| E | HOH663 |
| E | HOH675 |
| E | HOH688 |
| site_id | AD7 |
| Number of Residues | 3 |
| Details | binding site for residue EDO E 505 |
| Chain | Residue |
| A | SER173 |
| E | ASP343 |
| E | PHE345 |
| site_id | AD8 |
| Number of Residues | 5 |
| Details | binding site for residue EDO E 506 |
| Chain | Residue |
| A | ASP149 |
| A | PHE150 |
| A | TYR188 |
| E | THR349 |
| E | SER351 |
| site_id | AD9 |
| Number of Residues | 6 |
| Details | binding site for residue EDO E 507 |
| Chain | Residue |
| A | ILE360 |
| E | LEU191 |
| E | LYS201 |
| E | VAL202 |
| E | HIS203 |
| E | HOH707 |
| site_id | AE1 |
| Number of Residues | 4 |
| Details | binding site for residue EDO E 508 |
| Chain | Residue |
| E | PHE342 |
| E | ASP343 |
| E | THR346 |
| E | TYR391 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 20 |
| Details | Motif: {"description":"Zinc knuckle motif","evidences":[{"source":"PubMed","id":"24043831","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"25550159","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"26975377","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 6 |
| Details | Active site: {"evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 10 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"24043831","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"31479243","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"31479243","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6R4S","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"24043831","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"25550159","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"26975377","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"31479243","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 12 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"24043831","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"24239947","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"31479243","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"31479243","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |






