6RB4
Crystal structure of the Pri1 subunit of human primase
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 |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 7 |
Details | binding site for residue EDO A 501 |
Chain | Residue |
A | PHE150 |
A | PHE152 |
A | SER173 |
A | ARG329 |
A | HOH633 |
A | HOH657 |
A | HOH728 |
site_id | AC2 |
Number of Residues | 5 |
Details | binding site for residue EDO A 502 |
Chain | Residue |
A | ARG155 |
A | ASN401 |
A | HOH762 |
A | LYS153 |
A | HIS154 |
site_id | AC3 |
Number of Residues | 5 |
Details | binding site for residue EDO A 503 |
Chain | Residue |
A | PHE150 |
A | PHE345 |
A | HOH633 |
A | HOH698 |
A | HOH732 |
site_id | AC4 |
Number of Residues | 5 |
Details | binding site for residue EDO A 504 |
Chain | Residue |
A | GLU206 |
A | ASN281 |
A | ASN282 |
A | ASN285 |
A | HOH650 |
site_id | AC5 |
Number of Residues | 4 |
Details | binding site for residue ZN A 505 |
Chain | Residue |
A | CYS121 |
A | CYS122 |
A | CYS128 |
A | CYS131 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 10 |
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 | 3 |
Details | Active site: {"evidences":[{"evidenceCode":"ECO:0000255"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI3 |
Number of Residues | 5 |
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 | 3 |
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 | 4 |
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 | 6 |
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 | 1 |
Details | Binding site: {"evidences":[{"source":"PubMed","id":"31479243","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI8 |
Number of Residues | 1 |
Details | Modified residue: {"description":"N-acetylmethionine","evidences":[{"source":"PubMed","id":"22223895","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |