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 |






