6R4S
Crystal structure of the Pri1 subunit of human primase bound to ATP
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 | 0016779 | molecular_function | nucleotidyltransferase activity |
| A | 0032553 | molecular_function | ribonucleotide binding |
| A | 0046872 | molecular_function | metal ion binding |
| A | 1990077 | cellular_component | primosome complex |
| E | 0000287 | molecular_function | magnesium ion binding |
| E | 0000428 | cellular_component | DNA-directed RNA polymerase complex |
| E | 0003896 | molecular_function | DNA primase 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 | 0016779 | molecular_function | nucleotidyltransferase activity |
| E | 0032553 | molecular_function | ribonucleotide binding |
| E | 0046872 | molecular_function | metal ion binding |
| E | 1990077 | cellular_component | primosome complex |
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 | HIS166 |
| A | ATP504 |
| A | HOH608 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | binding site for residue MN A 503 |
| Chain | Residue |
| A | ASP109 |
| A | ASP111 |
| A | ASP306 |
| A | ATP504 |
| site_id | AC4 |
| Number of Residues | 15 |
| Details | binding site for residue ATP A 504 |
| Chain | Residue |
| A | ASP79 |
| A | ASP109 |
| A | ASP111 |
| A | SER160 |
| A | ARG162 |
| A | ARG163 |
| A | HIS166 |
| A | LEU316 |
| A | LEU317 |
| A | LYS318 |
| A | HIS324 |
| A | MN502 |
| A | MN503 |
| A | HOH608 |
| A | HOH610 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | binding site for residue ZN E 501 |
| Chain | Residue |
| E | CYS121 |
| E | CYS122 |
| E | CYS128 |
| E | CYS131 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | binding site for residue MN E 502 |
| Chain | Residue |
| E | ASP109 |
| E | ASP111 |
| E | HIS166 |
| E | ATP504 |
| E | HOH604 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | binding site for residue MN E 503 |
| Chain | Residue |
| E | ASP109 |
| E | ASP111 |
| E | ASP306 |
| E | ATP504 |
| site_id | AC8 |
| Number of Residues | 15 |
| Details | binding site for residue ATP E 504 |
| Chain | Residue |
| E | TYR54 |
| E | LYS77 |
| E | ASP79 |
| E | ASP109 |
| E | ASP111 |
| E | SER160 |
| E | ARG162 |
| E | ARG163 |
| E | HIS166 |
| E | LEU316 |
| E | LEU317 |
| E | LYS318 |
| E | HIS324 |
| E | MN502 |
| E | MN503 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 6 |
| Details | ACT_SITE: ACT_SITE => ECO:0000255 |
| Chain | Residue | Details |
| E | ASP109 | |
| E | ASP111 | |
| A | GLU44 | |
| A | ASP109 | |
| A | ASP111 | |
| E | GLU44 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 6 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:31479243, ECO:0007744|PDB:6R4S |
| Chain | Residue | Details |
| A | ASP306 | |
| E | ASP109 | |
| E | ASP111 | |
| E | ASP306 | |
| A | ASP109 | |
| A | ASP111 |
| 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 |
| E | CYS128 | |
| E | CYS131 | |
| A | CYS121 | |
| A | CYS122 | |
| A | CYS128 | |
| A | CYS131 | |
| E | CYS121 | |
| E | CYS122 |
| 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 | |
| E | 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 | |
| E | HIS315 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:31479243 |
| Chain | Residue | Details |
| A | HIS324 | |
| E | HIS324 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 2 |
| Details | MOD_RES: N-acetylmethionine => ECO:0007744|PubMed:22223895 |
| Chain | Residue | Details |
| A | MET1 | |
| E | MET1 |
