Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

3ZM7

CRYSTAL STRUCTURE OF THE ATPASE REGION OF Mycobacterium tuberculosis GyrB WITH AMPPCP

Functional Information from GO Data
ChainGOidnamespacecontents
A0003677molecular_functionDNA binding
A0003918molecular_functionDNA topoisomerase type II (double strand cut, ATP-hydrolyzing) activity
A0005524molecular_functionATP binding
A0006265biological_processDNA topological change
B0003677molecular_functionDNA binding
B0003918molecular_functionDNA topoisomerase type II (double strand cut, ATP-hydrolyzing) activity
B0005524molecular_functionATP binding
B0006265biological_processDNA topological change
C0003677molecular_functionDNA binding
C0003918molecular_functionDNA topoisomerase type II (double strand cut, ATP-hydrolyzing) activity
C0005524molecular_functionATP binding
C0006265biological_processDNA topological change
D0003677molecular_functionDNA binding
D0003918molecular_functionDNA topoisomerase type II (double strand cut, ATP-hydrolyzing) activity
D0005524molecular_functionATP binding
D0006265biological_processDNA topological change
E0003677molecular_functionDNA binding
E0003918molecular_functionDNA topoisomerase type II (double strand cut, ATP-hydrolyzing) activity
E0005524molecular_functionATP binding
E0006265biological_processDNA topological change
F0003677molecular_functionDNA binding
F0003918molecular_functionDNA topoisomerase type II (double strand cut, ATP-hydrolyzing) activity
F0005524molecular_functionATP binding
F0006265biological_processDNA topological change
Functional Information from PDB Data
site_idAC1
Number of Residues13
DetailsBINDING SITE FOR RESIDUE ACP A 525
ChainResidue
AGLU48
ASER169
AMG526
AHOH2004
AHOH2005
AASN52
AGLU56
AASP79
AGLY83
AILE84
AVAL99
AGLY124
AVAL125

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MG A 526
ChainResidue
AGLU48
AASN52
AACP525
AHOH2004

site_idAC3
Number of Residues11
DetailsBINDING SITE FOR RESIDUE ACP B 525
ChainResidue
BASN52
BGLU56
BILE84
BVAL99
BVAL123
BGLY124
BVAL125
BSER169
BMG526
BHOH2002
BHOH2003

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MG B 526
ChainResidue
BASN52
BACP525
BHOH2002
BHOH2003

site_idAC5
Number of Residues13
DetailsBINDING SITE FOR RESIDUE ACP C 525
ChainResidue
CGLU48
CASN52
CGLU56
CASP79
CGLY83
CILE84
CVAL123
CGLY124
CVAL125
CSER169
CMG526
CHOH2001
CHOH2002

site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG C 526
ChainResidue
CGLU48
CASN52
CACP525
CHOH2001
CHOH2002

site_idAC7
Number of Residues13
DetailsBINDING SITE FOR RESIDUE ACP D 525
ChainResidue
DGLU48
DASN52
DGLU56
DASP79
DGLY83
DILE84
DVAL99
DGLY122
DGLY124
DVAL125
DSER169
DMG526
DHOH2001

site_idAC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MG D 526
ChainResidue
DASN52
DACP525
DHOH2001
DHOH2002

site_idAC9
Number of Residues12
DetailsBINDING SITE FOR RESIDUE ACP E 525
ChainResidue
EGLU48
EASN52
EGLU56
EGLY83
EILE84
EVAL99
EGLY124
EVAL125
ESER169
EMG526
EHOH2003
EHOH2004

site_idBC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MG E 526
ChainResidue
EASN52
EACP525
EHOH2003
EHOH2004

site_idBC2
Number of Residues11
DetailsBINDING SITE FOR RESIDUE ACP F 525
ChainResidue
FGLU48
FASN52
FGLU56
FASP79
FILE84
FVAL99
FVAL123
FGLY124
FVAL125
FSER169
FMG526

site_idBC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG F 526
ChainResidue
FGLU48
FASN52
FGLY124
FVAL125
FACP525

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues28
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"24015710","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

238895

PDB entries from 2025-07-16

PDB statisticsPDBj update infoContact PDBjnumon