3ZKD
CRYSTAL STRUCTURE OF THE ATPASE REGION OF Mycobacterium tuberculosis GyrB WITH AMPPNP
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 |
| G | 0003677 | molecular_function | DNA binding |
| G | 0003918 | molecular_function | DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) activity |
| G | 0005524 | molecular_function | ATP binding |
| G | 0006265 | biological_process | DNA topological change |
| H | 0003677 | molecular_function | DNA binding |
| H | 0003918 | molecular_function | DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) activity |
| H | 0005524 | molecular_function | ATP binding |
| H | 0006265 | biological_process | DNA topological change |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 30 |
| Details | BINDING SITE FOR RESIDUE ANP A 601 |
| Chain | Residue |
| A | ASN52 |
| A | TYR114 |
| A | GLY119 |
| A | LEU120 |
| A | HIS121 |
| A | GLY122 |
| A | VAL123 |
| A | GLY124 |
| A | VAL125 |
| A | SER126 |
| A | SER169 |
| A | GLU56 |
| A | GLN370 |
| A | LYS372 |
| A | MG602 |
| A | HOH2004 |
| A | HOH2006 |
| A | HOH2008 |
| A | HOH2010 |
| A | HOH2011 |
| A | HOH2012 |
| B | TYR12 |
| A | ASP79 |
| B | ILE17 |
| A | GLY83 |
| A | ILE84 |
| A | VAL99 |
| A | GLY106 |
| A | GLY107 |
| A | LYS108 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE MG A 602 |
| Chain | Residue |
| A | ASN52 |
| A | ANP601 |
| A | HOH2006 |
| site_id | AC3 |
| Number of Residues | 26 |
| Details | BINDING SITE FOR RESIDUE ANP B 601 |
| Chain | Residue |
| A | TYR12 |
| A | ILE17 |
| B | GLU48 |
| B | ASN52 |
| B | GLU56 |
| B | ASP79 |
| B | ILE84 |
| B | VAL99 |
| B | ALA105 |
| B | GLY106 |
| B | GLY107 |
| B | LYS108 |
| B | TYR114 |
| B | GLY119 |
| B | LEU120 |
| B | HIS121 |
| B | GLY122 |
| B | VAL123 |
| B | GLY124 |
| B | VAL125 |
| B | SER169 |
| B | GLN370 |
| B | LYS372 |
| B | MG602 |
| B | HOH2005 |
| B | HOH2007 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG B 602 |
| Chain | Residue |
| B | GLU48 |
| B | ASN52 |
| B | ANP601 |
| B | HOH2005 |
| site_id | AC5 |
| Number of Residues | 30 |
| Details | BINDING SITE FOR RESIDUE ANP C 601 |
| Chain | Residue |
| C | GLU48 |
| C | ASN52 |
| C | GLU56 |
| C | ASP79 |
| C | GLY83 |
| C | ILE84 |
| C | VAL99 |
| C | ALA105 |
| C | GLY106 |
| C | GLY107 |
| C | LYS108 |
| C | TYR114 |
| C | GLY119 |
| C | LEU120 |
| C | HIS121 |
| C | GLY122 |
| C | VAL123 |
| C | GLY124 |
| C | VAL125 |
| C | SER126 |
| C | SER169 |
| C | GLN370 |
| C | LYS372 |
| C | MG602 |
| C | HOH2004 |
| C | HOH2011 |
| C | HOH2012 |
| C | HOH2013 |
| D | TYR12 |
| D | ILE17 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG C 602 |
| Chain | Residue |
| C | ASN52 |
| C | GLY119 |
| C | ANP601 |
| C | HOH2004 |
| C | HOH2008 |
| site_id | AC7 |
| Number of Residues | 26 |
| Details | BINDING SITE FOR RESIDUE ANP D 601 |
| Chain | Residue |
| D | GLU48 |
| D | ASN52 |
| D | GLU56 |
| D | ASP79 |
| D | GLY83 |
| D | ILE84 |
| D | VAL99 |
| D | ALA105 |
| D | GLY106 |
| D | GLY107 |
| D | LYS108 |
| D | TYR114 |
| D | GLY119 |
| D | LEU120 |
| D | HIS121 |
| D | GLY122 |
| D | VAL123 |
| D | GLY124 |
| D | VAL125 |
| D | SER126 |
| D | SER169 |
| D | GLN370 |
| D | LYS372 |
| D | MG602 |
| D | HOH2002 |
| C | TYR12 |
| site_id | AC8 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE MG D 602 |
| Chain | Residue |
| D | ASN52 |
| D | ANP601 |
| site_id | AC9 |
| Number of Residues | 28 |
| Details | BINDING SITE FOR RESIDUE ANP E 601 |
| Chain | Residue |
| E | GLU48 |
| E | ASN52 |
| E | GLU56 |
| E | ASP79 |
| E | ILE84 |
| E | VAL99 |
| E | ALA105 |
| E | GLY106 |
| E | GLY107 |
| E | LYS108 |
| E | TYR114 |
| E | GLY119 |
| E | LEU120 |
| E | HIS121 |
| E | GLY122 |
| E | VAL123 |
| E | GLY124 |
| E | VAL125 |
| E | SER169 |
| E | GLN370 |
| E | LYS372 |
| E | MG602 |
| E | HOH2006 |
| E | HOH2007 |
| E | HOH2009 |
| E | HOH2012 |
| F | TYR12 |
| F | ILE17 |
| site_id | BC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG E 602 |
| Chain | Residue |
| E | GLU48 |
| E | ASN52 |
| E | ANP601 |
| E | HOH2006 |
| site_id | BC2 |
| Number of Residues | 30 |
| Details | BINDING SITE FOR RESIDUE ANP F 601 |
| Chain | Residue |
| E | TYR12 |
| E | ILE17 |
| F | GLU48 |
| F | ASN52 |
| F | GLU56 |
| F | ASP79 |
| F | GLY83 |
| F | ILE84 |
| F | VAL99 |
| F | ALA105 |
| F | GLY106 |
| F | GLY107 |
| F | LYS108 |
| F | TYR114 |
| F | GLY119 |
| F | LEU120 |
| F | HIS121 |
| F | GLY122 |
| F | VAL123 |
| F | GLY124 |
| F | VAL125 |
| F | SER126 |
| F | SER169 |
| F | GLN370 |
| F | LYS372 |
| F | MG602 |
| F | HOH2004 |
| F | HOH2005 |
| F | HOH2007 |
| F | HOH2009 |
| site_id | BC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE MG F 602 |
| Chain | Residue |
| F | GLU48 |
| F | ASN52 |
| F | ANP601 |
| site_id | BC4 |
| Number of Residues | 30 |
| Details | BINDING SITE FOR RESIDUE ANP G 601 |
| Chain | Residue |
| G | GLU48 |
| G | ASN52 |
| G | GLU56 |
| G | ASP79 |
| G | GLY83 |
| G | ILE84 |
| G | VAL99 |
| G | ALA105 |
| G | GLY106 |
| G | GLY107 |
| G | LYS108 |
| G | TYR114 |
| G | GLY119 |
| G | LEU120 |
| G | HIS121 |
| G | GLY122 |
| G | VAL123 |
| G | GLY124 |
| G | VAL125 |
| G | GLN370 |
| G | LYS372 |
| G | MG602 |
| G | HOH2002 |
| G | HOH2003 |
| G | HOH2005 |
| G | HOH2010 |
| G | HOH2011 |
| G | HOH2012 |
| H | TYR12 |
| H | ILE17 |
| site_id | BC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG G 602 |
| Chain | Residue |
| G | GLU48 |
| G | ASN52 |
| G | GLY124 |
| G | ANP601 |
| G | HOH2005 |
| site_id | BC6 |
| Number of Residues | 25 |
| Details | BINDING SITE FOR RESIDUE ANP H 601 |
| Chain | Residue |
| G | TYR12 |
| G | ILE17 |
| H | GLU48 |
| H | ASN52 |
| H | GLU56 |
| H | ASP79 |
| H | GLY83 |
| H | ILE84 |
| H | VAL99 |
| H | ALA105 |
| H | GLY107 |
| H | LYS108 |
| H | TYR114 |
| H | GLY119 |
| H | LEU120 |
| H | HIS121 |
| H | GLY122 |
| H | VAL123 |
| H | GLY124 |
| H | VAL125 |
| H | SER126 |
| H | SER169 |
| H | GLN370 |
| H | LYS372 |
| H | MG602 |
| site_id | BC7 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE MG H 602 |
| Chain | Residue |
| H | GLU48 |
| H | ASN52 |
| H | ANP601 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 72 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:24015710 |
| Chain | Residue | Details |
| A | TYR12 | |
| B | TYR12 | |
| B | ASN52 | |
| B | ASP79 | |
| B | GLY83 | |
| B | GLY107 | |
| B | TYR114 | |
| B | LEU120 | |
| B | SER169 | |
| B | GLN370 | |
| C | TYR12 | |
| A | ASN52 | |
| C | ASN52 | |
| C | ASP79 | |
| C | GLY83 | |
| C | GLY107 | |
| C | TYR114 | |
| C | LEU120 | |
| C | SER169 | |
| C | GLN370 | |
| D | TYR12 | |
| D | ASN52 | |
| A | ASP79 | |
| D | ASP79 | |
| D | GLY83 | |
| D | GLY107 | |
| D | TYR114 | |
| D | LEU120 | |
| D | SER169 | |
| D | GLN370 | |
| E | TYR12 | |
| E | ASN52 | |
| E | ASP79 | |
| A | GLY83 | |
| E | GLY83 | |
| E | GLY107 | |
| E | TYR114 | |
| E | LEU120 | |
| E | SER169 | |
| E | GLN370 | |
| F | TYR12 | |
| F | ASN52 | |
| F | ASP79 | |
| F | GLY83 | |
| A | GLY107 | |
| F | GLY107 | |
| F | TYR114 | |
| F | LEU120 | |
| F | SER169 | |
| F | GLN370 | |
| G | TYR12 | |
| G | ASN52 | |
| G | ASP79 | |
| G | GLY83 | |
| G | GLY107 | |
| A | TYR114 | |
| G | TYR114 | |
| G | LEU120 | |
| G | SER169 | |
| G | GLN370 | |
| H | TYR12 | |
| H | ASN52 | |
| H | ASP79 | |
| H | GLY83 | |
| H | GLY107 | |
| H | TYR114 | |
| A | LEU120 | |
| H | LEU120 | |
| H | SER169 | |
| H | GLN370 | |
| A | SER169 | |
| A | GLN370 |
