Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000166 | molecular_function | nucleotide binding |
A | 0001882 | molecular_function | nucleoside binding |
A | 0003676 | molecular_function | nucleic acid binding |
A | 0003677 | molecular_function | DNA binding |
A | 0003887 | molecular_function | DNA-directed DNA polymerase activity |
A | 0004527 | molecular_function | exonuclease activity |
A | 0006260 | biological_process | DNA replication |
A | 0039693 | biological_process | viral DNA genome replication |
A | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE MG A 3202 |
Chain | Residue |
A | ASP249 |
A | VAL250 |
A | ASP458 |
A | MG3203 |
A | TTP3204 |
A | HOH3274 |
A | HOH3523 |
A | HOH3525 |
site_id | AC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MG A 3203 |
Chain | Residue |
A | ASP458 |
A | MG3202 |
A | TTP3204 |
A | HOH3525 |
A | ASP249 |
site_id | AC3 |
Number of Residues | 21 |
Details | BINDING SITE FOR RESIDUE TTP A 3204 |
Chain | Residue |
A | LEU253 |
A | TYR254 |
A | LYS371 |
A | LYS383 |
A | ASN387 |
A | ASP458 |
A | MG3202 |
A | MG3203 |
A | HOH3233 |
A | HOH3235 |
A | HOH3265 |
A | HOH3274 |
A | HOH3300 |
A | HOH3501 |
A | HOH3523 |
A | HOH3524 |
A | HOH3525 |
A | HOH3527 |
X | 2DA11 |
Y | DA6 |
Y | DT7 |
site_id | AC4 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE EDO A 1001 |
Chain | Residue |
A | ILE158 |
A | GLU291 |
A | EDO1004 |
site_id | AC5 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE EDO A 1002 |
Chain | Residue |
A | GLN257 |
A | SER260 |
A | THR440 |
A | GLY481 |
A | HOH3504 |
site_id | AC6 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE EDO A 1003 |
Chain | Residue |
A | LYS80 |
A | PRO87 |
A | ASN88 |
site_id | AC7 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE EDO A 1004 |
Chain | Residue |
A | ILE40 |
A | ASN42 |
A | ILE158 |
A | ASN344 |
A | EDO1001 |
site_id | AC8 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE EDO A 1005 |
Chain | Residue |
A | TYR59 |
A | ASP186 |
A | ARG187 |
A | MET188 |
site_id | AC9 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE EDO A 1006 |
Chain | Residue |
A | LYS124 |
A | THR189 |
A | GLY191 |
A | HOH3318 |
Y | DA6 |
Functional Information from PROSITE/UniProt
site_id | PS00116 |
Number of Residues | 9 |
Details | DNA_POLYMERASE_B DNA polymerase family B signature. YCDTDSIHL |
Chain | Residue | Details |
A | TYR454-LEU462 | |
Functional Information from SwissProt/UniProt
Chain | Residue | Details |
A | ASP145 | |
A | ASP169 | |
Chain | Residue | Details |
A | ASP249 | |
Chain | Residue | Details |
A | VAL250 | |
Chain | Residue | Details |
A | TYR254 | |
A | LYS371 | |
A | LYS383 | |
A | ASP458 | |
Chain | Residue | Details |
A | ASP456 | |
Chain | Residue | Details |
A | ALA12 | |
A | GLU14 | |
A | ALA66 | |
site_id | SWS_FT_FI7 |
Number of Residues | 2 |
Details | SITE: Involved in proofreading function by stabilization of the frayed primer-terminus at the 3'-5' exonuclease active site => ECO:0000269|PubMed:8605889 |
Chain | Residue | Details |
A | THR15 | |
A | ASN62 | |
Chain | Residue | Details |
A | TYR59 | |
A | HIS61 | |
A | PHE69 | |
site_id | SWS_FT_FI9 |
Number of Residues | 3 |
Details | SITE: Binds ssDNA; Essential for 3'-5' exonucleolysis => ECO:0000269|PubMed:9786901 |
Chain | Residue | Details |
A | PHE65 | |
A | SER122 | |
A | LEU123 | |
site_id | SWS_FT_FI10 |
Number of Residues | 1 |
Details | SITE: Involved in binding template-primer structures => ECO:0000269|PubMed:8344956 |
Chain | Residue | Details |
A | ILE93 | |
site_id | SWS_FT_FI11 |
Number of Residues | 1 |
Details | SITE: Involved in the stabilization of the frayed 3' terminus at the exonuclease active site => ECO:0000269|PubMed:19576228 |
Chain | Residue | Details |
A | TYR148 | |
site_id | SWS_FT_FI12 |
Number of Residues | 1 |
Details | SITE: Probably involved in binding template-primer structures => ECO:0000269|PubMed:8226957 |
Chain | Residue | Details |
A | SER252 | |
site_id | SWS_FT_FI13 |
Number of Residues | 2 |
Details | SITE: Probably involved in nucleotide binding selection => ECO:0000269|PubMed:8537389 |
Chain | Residue | Details |
A | TYR254 | |
A | TYR390 | |
site_id | SWS_FT_FI14 |
Number of Residues | 2 |
Details | SITE: Binds ssDNA; Essential for 3'-5' exonucleolysis => ECO:0000269|PubMed:8605889 |
Chain | Residue | Details |
A | THR356 | |
A | GLU420 | |
Chain | Residue | Details |
A | ILE364 | |
Chain | Residue | Details |
A | LYS366 | |
A | LYS379 | |
site_id | SWS_FT_FI17 |
Number of Residues | 1 |
Details | SITE: Interacts with the phosphate groups of the incoming nucleotide => ECO:0000269|PubMed:11917008 |
Chain | Residue | Details |
A | LYS371 | |
site_id | SWS_FT_FI18 |
Number of Residues | 1 |
Details | SITE: Probably involved in nucleotide binding selection => ECO:0000269|PubMed:9199402 |
Chain | Residue | Details |
A | LYS383 | |
site_id | SWS_FT_FI19 |
Number of Residues | 1 |
Details | SITE: Probably involved in positioning the templating nucleotide at the polymerization active site and in controlling nucleotide insertion fidelity => ECO:0000269|PubMed:12805385 |
Chain | Residue | Details |
A | LEU384 | |
site_id | SWS_FT_FI20 |
Number of Residues | 2 |
Details | SITE: Probably involved in binding template-primer structures => ECO:0000269|PubMed:8344956 |
Chain | Residue | Details |
A | ASN387 | |
A | GLY391 | |
site_id | SWS_FT_FI21 |
Number of Residues | 2 |
Details | SITE: Probably involved in binding template-primer structures => ECO:0000269|PubMed:7962004 |
Chain | Residue | Details |
A | THR434 | |
A | ARG438 | |
site_id | SWS_FT_FI22 |
Number of Residues | 2 |
Details | SITE: Probably involved in binding template-primer structures => ECO:0000269|PubMed:7852344 |
Chain | Residue | Details |
A | LYS498 | |
A | TYR500 | |
site_id | SWS_FT_FI23 |
Number of Residues | 1 |
Details | SITE: Stabilizes the primer-terminus at the polymerization active site and contributes to the coordination between the exonuclease and polymerazation activities => ECO:0000269|PubMed:24023769 |
Chain | Residue | Details |
A | LYS529 | |