4MM2
Crystal structure of yeast primase catalytic subunit
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000428 | cellular_component | DNA-directed RNA polymerase complex |
A | 0003697 | molecular_function | single-stranded DNA binding |
A | 0003896 | molecular_function | DNA primase activity |
A | 0005524 | molecular_function | ATP binding |
A | 0005658 | cellular_component | alpha DNA polymerase:primase complex |
A | 0006260 | biological_process | DNA replication |
A | 0006261 | biological_process | DNA-templated 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 | 0016779 | molecular_function | nucleotidyltransferase activity |
A | 0043596 | cellular_component | nuclear replication fork |
A | 0046872 | molecular_function | metal ion binding |
A | 1990077 | cellular_component | primosome complex |
B | 0000428 | cellular_component | DNA-directed RNA polymerase complex |
B | 0003697 | molecular_function | single-stranded DNA binding |
B | 0003896 | molecular_function | DNA primase activity |
B | 0005524 | molecular_function | ATP binding |
B | 0005658 | cellular_component | alpha DNA polymerase:primase complex |
B | 0006260 | biological_process | DNA replication |
B | 0006261 | biological_process | DNA-templated DNA replication |
B | 0006269 | biological_process | DNA replication, synthesis of primer |
B | 0006270 | biological_process | DNA replication initiation |
B | 0008270 | molecular_function | zinc ion binding |
B | 0016779 | molecular_function | nucleotidyltransferase activity |
B | 0043596 | cellular_component | nuclear replication fork |
B | 0046872 | molecular_function | metal ion binding |
B | 1990077 | cellular_component | primosome complex |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE CD A 501 |
Chain | Residue |
A | CYS123 |
A | CYS124 |
A | CYS130 |
A | CYS133 |
site_id | AC2 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE CD A 502 |
Chain | Residue |
A | HOH633 |
A | HOH646 |
A | ASP111 |
A | ASP113 |
A | HIS168 |
A | CD503 |
A | CIT506 |
site_id | AC3 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE CD A 503 |
Chain | Residue |
A | ASP111 |
A | ASP113 |
A | ASP314 |
A | CD502 |
site_id | AC4 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE CD A 504 |
Chain | Residue |
A | CYS123 |
A | CYS124 |
site_id | AC5 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE CD A 505 |
Chain | Residue |
A | CYS130 |
site_id | AC6 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE CIT A 506 |
Chain | Residue |
A | ARG79 |
A | SER162 |
A | ARG164 |
A | ARG165 |
A | GLY166 |
A | LYS326 |
A | HIS332 |
A | CD502 |
A | HOH626 |
A | HOH646 |
site_id | AC7 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE CD B 501 |
Chain | Residue |
B | CYS123 |
B | CYS124 |
B | CYS130 |
B | CYS133 |
site_id | AC8 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE CD B 502 |
Chain | Residue |
B | ASP111 |
B | ASP113 |
B | HIS168 |
B | CD503 |
B | CIT506 |
site_id | AC9 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE CD B 503 |
Chain | Residue |
B | ASP111 |
B | ASP113 |
B | ASP314 |
B | CD502 |
site_id | BC1 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE CD B 504 |
Chain | Residue |
B | CYS123 |
B | CYS124 |
B | HOH650 |
B | HOH805 |
site_id | BC2 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE CD B 505 |
Chain | Residue |
B | CYS130 |
B | HOH807 |
site_id | BC3 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE CIT B 506 |
Chain | Residue |
B | ARG79 |
B | ASP113 |
B | SER162 |
B | ARG164 |
B | ARG165 |
B | GLY166 |
B | LYS326 |
B | HIS332 |
B | CD502 |
B | HOH645 |
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 | GLU46 | |
A | ASP111 | |
A | ASP113 | |
B | GLU46 | |
B | ASP111 | |
B | ASP113 |