3ZM7
CRYSTAL STRUCTURE OF THE ATPASE REGION OF Mycobacterium tuberculosis GyrB WITH AMPPCP
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 | 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 | 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 |
E | 0003677 | molecular_function | DNA binding |
E | 0003918 | molecular_function | DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) activity |
E | 0005524 | molecular_function | ATP binding |
E | 0006265 | biological_process | DNA topological change |
F | 0003677 | molecular_function | DNA binding |
F | 0003918 | molecular_function | DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) activity |
F | 0005524 | molecular_function | ATP binding |
F | 0006265 | biological_process | DNA topological change |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 13 |
Details | BINDING SITE FOR RESIDUE ACP A 525 |
Chain | Residue |
A | GLU48 |
A | SER169 |
A | MG526 |
A | HOH2004 |
A | HOH2005 |
A | ASN52 |
A | GLU56 |
A | ASP79 |
A | GLY83 |
A | ILE84 |
A | VAL99 |
A | GLY124 |
A | VAL125 |
site_id | AC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE MG A 526 |
Chain | Residue |
A | GLU48 |
A | ASN52 |
A | ACP525 |
A | HOH2004 |
site_id | AC3 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE ACP B 525 |
Chain | Residue |
B | ASN52 |
B | GLU56 |
B | ILE84 |
B | VAL99 |
B | VAL123 |
B | GLY124 |
B | VAL125 |
B | SER169 |
B | MG526 |
B | HOH2002 |
B | HOH2003 |
site_id | AC4 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE MG B 526 |
Chain | Residue |
B | ASN52 |
B | ACP525 |
B | HOH2002 |
B | HOH2003 |
site_id | AC5 |
Number of Residues | 13 |
Details | BINDING SITE FOR RESIDUE ACP C 525 |
Chain | Residue |
C | GLU48 |
C | ASN52 |
C | GLU56 |
C | ASP79 |
C | GLY83 |
C | ILE84 |
C | VAL123 |
C | GLY124 |
C | VAL125 |
C | SER169 |
C | MG526 |
C | HOH2001 |
C | HOH2002 |
site_id | AC6 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MG C 526 |
Chain | Residue |
C | GLU48 |
C | ASN52 |
C | ACP525 |
C | HOH2001 |
C | HOH2002 |
site_id | AC7 |
Number of Residues | 13 |
Details | BINDING SITE FOR RESIDUE ACP D 525 |
Chain | Residue |
D | GLU48 |
D | ASN52 |
D | GLU56 |
D | ASP79 |
D | GLY83 |
D | ILE84 |
D | VAL99 |
D | GLY122 |
D | GLY124 |
D | VAL125 |
D | SER169 |
D | MG526 |
D | HOH2001 |
site_id | AC8 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE MG D 526 |
Chain | Residue |
D | ASN52 |
D | ACP525 |
D | HOH2001 |
D | HOH2002 |
site_id | AC9 |
Number of Residues | 12 |
Details | BINDING SITE FOR RESIDUE ACP E 525 |
Chain | Residue |
E | GLU48 |
E | ASN52 |
E | GLU56 |
E | GLY83 |
E | ILE84 |
E | VAL99 |
E | GLY124 |
E | VAL125 |
E | SER169 |
E | MG526 |
E | HOH2003 |
E | HOH2004 |
site_id | BC1 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE MG E 526 |
Chain | Residue |
E | ASN52 |
E | ACP525 |
E | HOH2003 |
E | HOH2004 |
site_id | BC2 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE ACP F 525 |
Chain | Residue |
F | GLU48 |
F | ASN52 |
F | GLU56 |
F | ASP79 |
F | ILE84 |
F | VAL99 |
F | VAL123 |
F | GLY124 |
F | VAL125 |
F | SER169 |
F | MG526 |
site_id | BC3 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MG F 526 |
Chain | Residue |
F | GLU48 |
F | ASN52 |
F | GLY124 |
F | VAL125 |
F | ACP525 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 28 |
Details | Binding site: {"evidences":[{"source":"PubMed","id":"24015710","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |