Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0003684 | molecular_function | damaged DNA binding |
A | 0003887 | molecular_function | DNA-directed DNA polymerase activity |
A | 0006281 | biological_process | DNA repair |
B | 0003684 | molecular_function | damaged DNA binding |
B | 0003887 | molecular_function | DNA-directed DNA polymerase activity |
B | 0006281 | biological_process | DNA repair |
C | 0003684 | molecular_function | damaged DNA binding |
C | 0003887 | molecular_function | DNA-directed DNA polymerase activity |
C | 0006281 | biological_process | DNA repair |
D | 0003684 | molecular_function | damaged DNA binding |
D | 0003887 | molecular_function | DNA-directed DNA polymerase activity |
D | 0006281 | biological_process | DNA repair |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 17 |
Details | BINDING SITE FOR RESIDUE DCP A 101 |
Chain | Residue |
A | HOH89 |
A | PHE428 |
A | ALA509 |
A | SER510 |
A | TYR513 |
A | ARG516 |
A | ASN522 |
A | ASP570 |
A | LYS625 |
A | MG201 |
A | MG202 |
A | ARG357 |
A | ASP423 |
A | MET424 |
A | ASP425 |
A | CYS426 |
A | PHE427 |
site_id | AC2 |
Number of Residues | 14 |
Details | BINDING SITE FOR RESIDUE DCP B 101 |
Chain | Residue |
B | MG203 |
B | ARG357 |
B | ASP423 |
B | MET424 |
B | CYS426 |
B | PHE427 |
B | PHE428 |
B | ALA509 |
B | SER510 |
B | TYR513 |
B | ARG516 |
B | ASN522 |
B | ASP570 |
B | LYS625 |
site_id | AC3 |
Number of Residues | 19 |
Details | BINDING SITE FOR RESIDUE DCP C 101 |
Chain | Residue |
C | HOH73 |
C | HOH87 |
C | MG205 |
C | MG206 |
C | ARG357 |
C | ASP423 |
C | MET424 |
C | ASP425 |
C | CYS426 |
C | PHE427 |
C | PHE428 |
C | ALA509 |
C | SER510 |
C | TYR513 |
C | ARG516 |
C | ASN522 |
C | ASP570 |
C | LYS625 |
I | DOC12 |
site_id | AC4 |
Number of Residues | 16 |
Details | BINDING SITE FOR RESIDUE DCP D 101 |
Chain | Residue |
D | MG207 |
D | MG208 |
D | ARG357 |
D | ASP423 |
D | MET424 |
D | ASP425 |
D | CYS426 |
D | PHE427 |
D | PHE428 |
D | ALA509 |
D | SER510 |
D | TYR513 |
D | ARG516 |
D | ASN522 |
D | ASP570 |
D | LYS625 |
site_id | AC5 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE MG A 201 |
Chain | Residue |
A | DCP101 |
A | ASP423 |
A | MET424 |
A | ASP570 |
site_id | AC6 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MG A 202 |
Chain | Residue |
A | DCP101 |
A | SER568 |
A | ASP570 |
A | GLU571 |
E | DOC12 |
site_id | AC7 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE MG B 203 |
Chain | Residue |
B | DCP101 |
B | ASP423 |
B | MET424 |
B | ASP570 |
site_id | AC8 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE MG C 205 |
Chain | Residue |
C | DCP101 |
C | ASP423 |
C | MET424 |
C | ASP570 |
site_id | AC9 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MG C 206 |
Chain | Residue |
C | DCP101 |
C | SER568 |
C | ASP570 |
C | GLU571 |
I | DOC12 |
site_id | BC1 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MG D 207 |
Chain | Residue |
D | DCP101 |
D | MG208 |
D | ASP423 |
D | MET424 |
D | ASP570 |
site_id | BC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MG D 208 |
Chain | Residue |
D | DCP101 |
D | MG207 |
D | ASP423 |
D | ASP570 |
D | GLU571 |
K | DOC12 |
site_id | BC3 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MG A 209 |
Chain | Residue |
A | THR447 |
A | SER448 |
A | GLU507 |
A | TYR541 |
F | DA3 |
site_id | BC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MG D 210 |
Chain | Residue |
D | THR447 |
D | SER448 |
D | GLU507 |
D | TYR541 |
L | DA3 |
site_id | BC5 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE MG A 211 |
Chain | Residue |
A | THR647 |
A | LEU649 |
A | VAL652 |
E | DA11 |
site_id | BC6 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MG B 212 |
Chain | Residue |
B | THR647 |
B | ASN648 |
B | LEU649 |
B | VAL652 |
G | DA11 |
site_id | BC7 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE MG C 213 |
Chain | Residue |
C | THR647 |
C | LEU649 |
C | VAL652 |
I | DA11 |
site_id | BC8 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MG D 214 |
Chain | Residue |
D | THR647 |
D | LEU649 |
D | VAL652 |
K | DA11 |
K | HOH75 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 12 |
Details | BINDING: BINDING => ECO:0000250 |
Chain | Residue | Details |
A | ARG357 | |
D | ARG357 | |
D | SER510 | |
D | ASN522 | |
A | SER510 | |
A | ASN522 | |
B | ARG357 | |
B | SER510 | |
B | ASN522 | |
C | ARG357 | |
C | SER510 | |
C | ASN522 | |
Chain | Residue | Details |
A | ASP423 | |
D | ASP423 | |
D | ASP570 | |
D | GLU571 | |
A | ASP570 | |
A | GLU571 | |
B | ASP423 | |
B | ASP570 | |
B | GLU571 | |
C | ASP423 | |
C | ASP570 | |
C | GLU571 | |
site_id | SWS_FT_FI3 |
Number of Residues | 8 |
Details | SITE: Interaction with target DNA => ECO:0000250 |
Chain | Residue | Details |
A | LYS770 | |
A | THR783 | |
B | LYS770 | |
B | THR783 | |
C | LYS770 | |
C | THR783 | |
D | LYS770 | |
D | THR783 | |