5CDO
3.15A structure of QPT-1 with S.aureus DNA gyrase and DNA
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0003677 | molecular_function | DNA binding |
A | 0003918 | molecular_function | DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) activity |
A | 0005524 | molecular_function | ATP binding |
A | 0006259 | biological_process | DNA metabolic process |
A | 0006265 | biological_process | DNA topological change |
B | 0003677 | molecular_function | DNA binding |
B | 0003918 | molecular_function | DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) activity |
B | 0005524 | molecular_function | ATP binding |
B | 0006265 | biological_process | DNA topological change |
C | 0003677 | molecular_function | DNA binding |
C | 0003918 | molecular_function | DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) activity |
C | 0005524 | molecular_function | ATP binding |
C | 0006259 | biological_process | DNA metabolic process |
C | 0006265 | biological_process | DNA topological change |
D | 0003677 | molecular_function | DNA binding |
D | 0003918 | molecular_function | DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) activity |
D | 0005524 | molecular_function | ATP binding |
D | 0006265 | biological_process | DNA topological change |
R | 0003677 | molecular_function | DNA binding |
R | 0003918 | molecular_function | DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) activity |
R | 0005524 | molecular_function | ATP binding |
R | 0006259 | biological_process | DNA metabolic process |
R | 0006265 | biological_process | DNA topological change |
S | 0003677 | molecular_function | DNA binding |
S | 0003918 | molecular_function | DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) activity |
S | 0005524 | molecular_function | ATP binding |
S | 0006265 | biological_process | DNA topological change |
T | 0003677 | molecular_function | DNA binding |
T | 0003918 | molecular_function | DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) activity |
T | 0005524 | molecular_function | ATP binding |
T | 0006259 | biological_process | DNA metabolic process |
T | 0006265 | biological_process | DNA topological change |
U | 0003677 | molecular_function | DNA binding |
U | 0003918 | molecular_function | DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) activity |
U | 0005524 | molecular_function | ATP binding |
U | 0006265 | biological_process | DNA topological change |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 2 |
Details | binding site for residue SO4 A 501 |
Chain | Residue |
A | ARG429 |
C | ARG429 |
site_id | AC2 |
Number of Residues | 4 |
Details | binding site for residue NA A 502 |
Chain | Residue |
A | TYR322 |
A | LYS323 |
A | THR325 |
A | GLN328 |
site_id | AC3 |
Number of Residues | 4 |
Details | binding site for residue GOL A 503 |
Chain | Residue |
A | PRO157 |
A | ARG47 |
A | ARG48 |
A | GLU156 |
site_id | AC4 |
Number of Residues | 6 |
Details | binding site for residue MN B 701 |
Chain | Residue |
B | ASP508 |
B | ASP510 |
B | HOH801 |
B | HOH802 |
B | HOH805 |
E | HOH2202 |
site_id | AC5 |
Number of Residues | 3 |
Details | binding site for residue NA C 501 |
Chain | Residue |
C | GLY152 |
C | ASN153 |
C | GLU154 |
site_id | AC6 |
Number of Residues | 4 |
Details | binding site for residue NA C 502 |
Chain | Residue |
C | TYR322 |
C | LYS323 |
C | THR325 |
C | GLN328 |
site_id | AC7 |
Number of Residues | 6 |
Details | binding site for residue MN D 1001 |
Chain | Residue |
D | ASP508 |
D | ASP510 |
D | HOH1101 |
D | HOH1102 |
D | HOH1103 |
D | HOH1104 |
site_id | AC8 |
Number of Residues | 4 |
Details | binding site for residue GOL D 1002 |
Chain | Residue |
D | ASN474 |
D | ASN475 |
D | ASN476 |
E | DG2013 |
site_id | AC9 |
Number of Residues | 3 |
Details | binding site for residue GOL D 1003 |
Chain | Residue |
A | SER297 |
D | SER445 |
D | GLY446 |
site_id | AD1 |
Number of Residues | 8 |
Details | binding site for residue 53M E 2101 |
Chain | Residue |
B | GLY436 |
B | ASP437 |
B | ARG458 |
C | PTR123 |
E | DC8 |
E | DG2009 |
F | DC2012 |
F | DG2013 |
site_id | AD2 |
Number of Residues | 10 |
Details | binding site for residue 53L F 2101 |
Chain | Residue |
A | PTR123 |
D | GLY436 |
D | ASP437 |
D | ARG458 |
D | GLY459 |
E | DC2012 |
E | DG2013 |
F | DC8 |
F | DG2009 |
F | HOH2202 |
site_id | AD3 |
Number of Residues | 3 |
Details | binding site for residue NA R 501 |
Chain | Residue |
R | TYR322 |
R | THR325 |
R | GLN328 |
site_id | AD4 |
Number of Residues | 6 |
Details | binding site for residue MN S 6001 |
Chain | Residue |
S | ASP508 |
S | ASP510 |
S | HOH6103 |
S | HOH6104 |
S | HOH6106 |
S | HOH6107 |
site_id | AD5 |
Number of Residues | 10 |
Details | binding site for residue 50M S 6002 |
Chain | Residue |
S | GLY436 |
S | ASP437 |
S | ARG458 |
S | GLY459 |
S | HOH6102 |
T | PTR123 |
V | DC2012 |
V | DG2013 |
W | DC8 |
W | DG2009 |
site_id | AD6 |
Number of Residues | 3 |
Details | binding site for residue SO4 T 501 |
Chain | Residue |
R | ARG429 |
T | ARG429 |
T | ARG432 |
site_id | AD7 |
Number of Residues | 5 |
Details | binding site for residue SO4 T 502 |
Chain | Residue |
T | PRO44 |
T | ARG47 |
T | GLU156 |
T | PRO157 |
T | SER158 |
site_id | AD8 |
Number of Residues | 4 |
Details | binding site for residue NA T 503 |
Chain | Residue |
T | TYR322 |
T | THR325 |
T | GLN328 |
T | HOH615 |
site_id | AD9 |
Number of Residues | 6 |
Details | binding site for residue MN U 5001 |
Chain | Residue |
U | ASP508 |
U | ASP510 |
U | HOH5101 |
U | HOH5102 |
U | HOH5107 |
V | HOH2102 |
site_id | AE1 |
Number of Residues | 2 |
Details | binding site for residue GOL U 5002 |
Chain | Residue |
U | ASN476 |
W | DG2013 |
site_id | AE2 |
Number of Residues | 3 |
Details | binding site for residue GOL U 5003 |
Chain | Residue |
U | GLY446 |
U | ARG447 |
U | TRP592 |
site_id | AE3 |
Number of Residues | 8 |
Details | binding site for residue 53M W 2101 |
Chain | Residue |
U | GLY459 |
V | DC8 |
V | DG2009 |
W | DC2012 |
W | DG2013 |
U | GLY436 |
U | ASP437 |
U | ARG458 |
Functional Information from PROSITE/UniProt
site_id | PS00177 |
Number of Residues | 9 |
Details | TOPOISOMERASE_II DNA topoisomerase II signature. LVEGDSAGG |
Chain | Residue | Details |
B | LEU433-GLY441 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 12 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01898 |
Chain | Residue | Details |
B | GLU435 | |
U | GLU435 | |
U | ASP508 | |
U | ASP510 | |
B | ASP508 | |
B | ASP510 | |
D | GLU435 | |
D | ASP508 | |
D | ASP510 | |
S | GLU435 | |
S | ASP508 | |
S | ASP510 |
site_id | SWS_FT_FI2 |
Number of Residues | 8 |
Details | SITE: Interaction with DNA => ECO:0000255|HAMAP-Rule:MF_01898 |
Chain | Residue | Details |
B | LYS460 | |
B | ASN463 | |
D | LYS460 | |
D | ASN463 | |
S | LYS460 | |
S | ASN463 | |
U | LYS460 | |
U | ASN463 |