4BPU
Crystal structure of human primase in heterodimeric form, comprising PriS and truncated PriL lacking the C-terminal Fe-S domain.
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 | 0003896 | molecular_function | DNA primase 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 |
| B | 0006269 | biological_process | DNA replication, synthesis of primer |
| C | 0000287 | molecular_function | magnesium ion binding |
| C | 0000428 | cellular_component | DNA-directed RNA polymerase complex |
| C | 0003896 | molecular_function | DNA primase activity |
| C | 0005515 | molecular_function | protein binding |
| C | 0005654 | cellular_component | nucleoplasm |
| C | 0005658 | cellular_component | alpha DNA polymerase:primase complex |
| C | 0006260 | biological_process | DNA replication |
| C | 0006269 | biological_process | DNA replication, synthesis of primer |
| C | 0006270 | biological_process | DNA replication initiation |
| C | 0008270 | molecular_function | zinc ion binding |
| C | 0016020 | cellular_component | membrane |
| C | 0016740 | molecular_function | transferase activity |
| C | 0016779 | molecular_function | nucleotidyltransferase activity |
| C | 0032553 | molecular_function | ribonucleotide binding |
| C | 0046872 | molecular_function | metal ion binding |
| D | 0006269 | biological_process | DNA replication, synthesis of primer |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A 1409 |
| Chain | Residue |
| A | CYS121 |
| A | CYS122 |
| A | CYS128 |
| A | CYS131 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN C 1409 |
| Chain | Residue |
| C | CYS121 |
| C | CYS122 |
| C | CYS128 |
| C | CYS131 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE GOL A 1410 |
| Chain | Residue |
| A | VAL118 |
| A | LYS242 |
| A | TYR300 |
| A | ASP117 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL A 1411 |
| Chain | Residue |
| A | GLU224 |
| A | TRP269 |
| A | LYS273 |
| A | GLU293 |
| A | MET297 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL A 1412 |
| Chain | Residue |
| A | LYS153 |
| A | HIS154 |
| A | ARG155 |
| A | PHE398 |
| A | ASN401 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL A 1413 |
| Chain | Residue |
| A | TYR159 |
| A | ARG329 |
| A | PRO344 |
| A | PHE345 |
| A | HOH2059 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 6 |
| Details | ACT_SITE: ACT_SITE => ECO:0000255 |
| Chain | Residue | Details |
| A | GLU44 | |
| A | ASP109 | |
| A | ASP111 | |
| C | GLU44 | |
| C | ASP109 | |
| C | ASP111 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 6 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:31479243, ECO:0007744|PDB:6R4S |
| Chain | Residue | Details |
| A | ASP109 | |
| A | ASP111 | |
| A | ASP306 | |
| C | ASP109 | |
| C | ASP111 | |
| C | ASP306 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 8 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:24043831, ECO:0000269|PubMed:25550159, ECO:0000269|PubMed:26975377, ECO:0000269|PubMed:31479243 |
| Chain | Residue | Details |
| A | CYS121 | |
| A | CYS122 | |
| A | CYS128 | |
| A | CYS131 | |
| C | CYS121 | |
| C | CYS122 | |
| C | CYS128 | |
| C | CYS131 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:24043831, ECO:0000269|PubMed:24239947, ECO:0000269|PubMed:31479243 |
| Chain | Residue | Details |
| A | SER160 | |
| C | SER160 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:24043831, ECO:0000269|PubMed:31479243 |
| Chain | Residue | Details |
| A | HIS315 | |
| C | HIS315 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:31479243 |
| Chain | Residue | Details |
| A | HIS324 | |
| C | HIS324 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 2 |
| Details | MOD_RES: N-acetylmethionine => ECO:0007744|PubMed:22223895 |
| Chain | Residue | Details |
| A | MET1 | |
| C | MET1 |
