3KD1
Closed binary complex of an RB69 gp43 fingers domain mutant complexed with an acyclic GMP terminated primer template pair.
Functional Information from GO Data
Chain | GOid | namespace | contents |
E | 0000166 | molecular_function | nucleotide binding |
E | 0003676 | molecular_function | nucleic acid binding |
E | 0003677 | molecular_function | DNA binding |
E | 0003887 | molecular_function | DNA-directed DNA polymerase activity |
E | 0004527 | molecular_function | exonuclease activity |
E | 0006260 | biological_process | DNA replication |
E | 0006261 | biological_process | DNA-templated DNA replication |
E | 0006287 | biological_process | base-excision repair, gap-filling |
E | 0006297 | biological_process | nucleotide-excision repair, DNA gap filling |
E | 0008296 | molecular_function | 3'-5'-DNA exonuclease activity |
E | 0008408 | molecular_function | 3'-5' exonuclease activity |
E | 0009432 | biological_process | SOS response |
E | 0039686 | biological_process | bidirectional double-stranded viral DNA replication |
E | 0039693 | biological_process | viral DNA genome replication |
E | 0045004 | biological_process | DNA replication proofreading |
E | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE MG E 914 |
Chain | Residue |
E | ASP114 |
E | ILE115 |
E | GLU116 |
E | HOH1091 |
Functional Information from PROSITE/UniProt
site_id | PS00116 |
Number of Residues | 9 |
Details | DNA_POLYMERASE_B DNA polymerase family B signature. YGDTDSIYV |
Chain | Residue | Details |
E | TYR619-VAL627 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_04100 |
Chain | Residue | Details |
E | ASP114 | |
E | GLU116 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_04100, ECO:0000305|PubMed:23214497 |
Chain | Residue | Details |
E | ALA222 | |
E | ASP327 |
Chain | Residue | Details |
E | ASP411 |
site_id | SWS_FT_FI4 |
Number of Residues | 1 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_04100, ECO:0000269|PubMed:17718515, ECO:0000269|PubMed:21566148, ECO:0000269|PubMed:21923197, ECO:0000305|PubMed:18503083, ECO:0000305|PubMed:23214497, ECO:0000305|PubMed:23921641, ECO:0007744|PDB:2OZM, ECO:0007744|PDB:2OZS, ECO:0007744|PDB:3KD5, ECO:0007744|PDB:3SI6, ECO:0007744|PDB:3SNN, ECO:0007744|PDB:3SPY |
Chain | Residue | Details |
E | LEU412 |
Chain | Residue | Details |
E | ARG482 | |
E | SER414 |
Chain | Residue | Details |
E | LYS560 |
Chain | Residue | Details |
E | ASP623 |
site_id | SWS_FT_FI8 |
Number of Residues | 1 |
Details | SITE: Optimization of metal coordination by the polymerase active site => ECO:0000255|HAMAP-Rule:MF_04100, ECO:0000305|PubMed:15057283, ECO:0000305|PubMed:20166752, ECO:0000305|PubMed:22571765, ECO:0000305|PubMed:24116139 |
Chain | Residue | Details |
E | ASP621 |
site_id | SWS_FT_FI9 |
Number of Residues | 1 |
Details | SITE: Optimization of metal coordination by the polymerase active site => ECO:0000255|HAMAP-Rule:MF_04100, ECO:0000269|PubMed:15057283, ECO:0000269|PubMed:22571765 |
Chain | Residue | Details |
E | LYS706 |
site_id | SWS_FT_FI10 |
Number of Residues | 1 |
Details | SITE: Essential for viral replication => ECO:0000255|HAMAP-Rule:MF_04100, ECO:0000269|PubMed:24116139 |
Chain | Residue | Details |
E | ASP714 |