1SL0
Ternary 3' complex of T7 DNA polymerase with a DNA primer/template containing a disordered cis-syn thymine dimer on the template and an incoming nucleotide
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 | 0004529 | molecular_function | DNA exonuclease activity |
A | 0005515 | molecular_function | protein binding |
A | 0006260 | biological_process | DNA replication |
A | 0006261 | biological_process | DNA-templated DNA replication |
A | 0006302 | biological_process | double-strand break repair |
A | 0008408 | molecular_function | 3'-5' exonuclease activity |
A | 0039693 | biological_process | viral DNA genome replication |
A | 0046872 | molecular_function | metal ion binding |
A | 0090592 | biological_process | DNA synthesis involved in DNA replication |
B | 0005515 | molecular_function | protein binding |
B | 0005737 | cellular_component | cytoplasm |
B | 0005829 | cellular_component | cytosol |
B | 0015035 | molecular_function | protein-disulfide reductase activity |
B | 0015036 | molecular_function | disulfide oxidoreductase activity |
B | 0030337 | molecular_function | DNA polymerase processivity factor activity |
B | 0045454 | biological_process | cell redox homeostasis |
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 | 0004529 | molecular_function | DNA exonuclease activity |
C | 0005515 | molecular_function | protein binding |
C | 0006260 | biological_process | DNA replication |
C | 0006261 | biological_process | DNA-templated DNA replication |
C | 0006302 | biological_process | double-strand break repair |
C | 0008408 | molecular_function | 3'-5' exonuclease activity |
C | 0039693 | biological_process | viral DNA genome replication |
C | 0046872 | molecular_function | metal ion binding |
C | 0090592 | biological_process | DNA synthesis involved in DNA replication |
D | 0005515 | molecular_function | protein binding |
D | 0005737 | cellular_component | cytoplasm |
D | 0005829 | cellular_component | cytosol |
D | 0015035 | molecular_function | protein-disulfide reductase activity |
D | 0015036 | molecular_function | disulfide oxidoreductase activity |
D | 0030337 | molecular_function | DNA polymerase processivity factor activity |
D | 0045454 | biological_process | cell redox homeostasis |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE MG A 4003 |
Chain | Residue |
A | ASP5 |
A | ASP65 |
site_id | AC2 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE MG C 4004 |
Chain | Residue |
C | ASP5 |
C | HIS59 |
C | ASP65 |
site_id | AC3 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE DAD C 4005 |
Chain | Residue |
C | HIS506 |
C | ARG518 |
site_id | AC4 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE DAD A 4004 |
Chain | Residue |
A | TYR526 |
A | HIS506 |
A | ARG518 |
Functional Information from PROSITE/UniProt
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 4 |
Details | ACT_SITE: Nucleophile |
Chain | Residue | Details |
B | GLY33 | |
B | LYS36 | |
D | GLY33 | |
D | LYS36 | |
C | GLU7 | |
C | ALA180 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | SITE: Deprotonates C-terminal active site Cys |
Chain | Residue | Details |
B | PHE27 | |
D | PHE27 | |
A | CYS660 | |
C | LEU481 | |
C | ARG482 | |
C | CYS660 |
site_id | SWS_FT_FI3 |
Number of Residues | 4 |
Details | SITE: Contributes to redox potential value |
Chain | Residue | Details |
B | PRO34 | |
B | CYS35 | |
D | PRO34 | |
D | CYS35 | |
C | ALA512 | |
C | PHE524 | |
C | PHE528 | |
C | ALA532 |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | MOD_RES: N6-acetyllysine => ECO:0000269|PubMed:18723842 |
Chain | Residue | Details |
B | TYR70 | |
D | TYR70 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1mek |
Chain | Residue | Details |
B | PRO34 | |
B | CYS35 | |
B | CYS32 | |
B | GLY33 |
site_id | CSA2 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1mek |
Chain | Residue | Details |
D | PRO34 | |
D | CYS35 | |
D | CYS32 | |
D | GLY33 |
site_id | CSA3 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1mek |
Chain | Residue | Details |
B | CYS35 | |
B | CYS32 |
site_id | CSA4 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1mek |
Chain | Residue | Details |
D | CYS35 | |
D | CYS32 |