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 | 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 | 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 | 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 |