3TAE
5-hydroxycytosine paired with dAMP in RB69 gp43
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000166 | molecular_function | nucleotide 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 | 0006261 | biological_process | DNA-templated DNA replication |
A | 0008408 | molecular_function | 3'-5' exonuclease activity |
A | 0039686 | biological_process | bidirectional double-stranded viral DNA replication |
A | 0039693 | biological_process | viral DNA genome replication |
A | 0046872 | molecular_function | metal ion binding |
B | 0000166 | molecular_function | nucleotide binding |
B | 0003676 | molecular_function | nucleic acid binding |
B | 0003677 | molecular_function | DNA binding |
B | 0003887 | molecular_function | DNA-directed DNA polymerase activity |
B | 0004527 | molecular_function | exonuclease activity |
B | 0006260 | biological_process | DNA replication |
B | 0006261 | biological_process | DNA-templated DNA replication |
B | 0008408 | molecular_function | 3'-5' exonuclease activity |
B | 0039686 | biological_process | bidirectional double-stranded viral DNA replication |
B | 0039693 | biological_process | viral DNA genome replication |
B | 0046872 | molecular_function | metal ion binding |
C | 0000166 | molecular_function | nucleotide binding |
C | 0003676 | molecular_function | nucleic acid binding |
C | 0003677 | molecular_function | DNA binding |
C | 0003887 | molecular_function | DNA-directed DNA polymerase activity |
C | 0004527 | molecular_function | exonuclease activity |
C | 0006260 | biological_process | DNA replication |
C | 0006261 | biological_process | DNA-templated DNA replication |
C | 0008408 | molecular_function | 3'-5' exonuclease activity |
C | 0039686 | biological_process | bidirectional double-stranded viral DNA replication |
C | 0039693 | biological_process | viral DNA genome replication |
C | 0046872 | molecular_function | metal ion binding |
D | 0000166 | molecular_function | nucleotide binding |
D | 0003676 | molecular_function | nucleic acid binding |
D | 0003677 | molecular_function | DNA binding |
D | 0003887 | molecular_function | DNA-directed DNA polymerase activity |
D | 0004527 | molecular_function | exonuclease activity |
D | 0006260 | biological_process | DNA replication |
D | 0006261 | biological_process | DNA-templated DNA replication |
D | 0008408 | molecular_function | 3'-5' exonuclease activity |
D | 0039686 | biological_process | bidirectional double-stranded viral DNA replication |
D | 0039693 | biological_process | viral DNA genome replication |
D | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE SO4 F 3 |
Chain | Residue |
F | DG101 |
F | DC102 |
site_id | AC2 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE SO4 H 2 |
Chain | Residue |
H | DG101 |
H | DC102 |
site_id | AC3 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE SO4 B 907 |
Chain | Residue |
B | HIS40 |
B | GLY79 |
B | LEU80 |
B | GLU81 |
B | HOH952 |
site_id | AC4 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE SO4 C 907 |
Chain | Residue |
C | HIS105 |
C | ASN342 |
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 |
A | TYR619-VAL627 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 8 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_04100 |
Chain | Residue | Details |
A | ASP114 | |
A | GLU116 | |
B | ASP114 | |
B | GLU116 | |
C | ASP114 | |
C | GLU116 | |
D | ASP114 | |
D | GLU116 |
site_id | SWS_FT_FI2 |
Number of Residues | 8 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_04100, ECO:0000305|PubMed:23214497 |
Chain | Residue | Details |
A | ALA222 | |
A | ALA327 | |
B | ALA222 | |
B | ALA327 | |
C | ALA222 | |
C | ALA327 | |
D | ALA222 | |
D | ALA327 |
Chain | Residue | Details |
A | ASP411 | |
B | ASP411 | |
C | ASP411 | |
D | ASP411 |
site_id | SWS_FT_FI4 |
Number of Residues | 4 |
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 |
A | LEU412 | |
B | LEU412 | |
C | LEU412 | |
D | LEU412 |
Chain | Residue | Details |
A | SER414 | |
A | ARG482 | |
B | SER414 | |
B | ARG482 | |
C | SER414 | |
C | ARG482 | |
D | SER414 | |
D | ARG482 |
Chain | Residue | Details |
A | LYS560 | |
B | LYS560 | |
C | LYS560 | |
D | LYS560 |
Chain | Residue | Details |
A | ASP623 | |
B | ASP623 | |
C | ASP623 | |
D | ASP623 |
site_id | SWS_FT_FI8 |
Number of Residues | 4 |
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 |
A | ASP621 | |
B | ASP621 | |
C | ASP621 | |
D | ASP621 |
site_id | SWS_FT_FI9 |
Number of Residues | 4 |
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 |
A | LYS706 | |
B | LYS706 | |
C | LYS706 | |
D | LYS706 |
site_id | SWS_FT_FI10 |
Number of Residues | 4 |
Details | SITE: Essential for viral replication => ECO:0000255|HAMAP-Rule:MF_04100, ECO:0000269|PubMed:24116139 |
Chain | Residue | Details |
A | ASP714 | |
B | ASP714 | |
C | ASP714 | |
D | ASP714 |