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

8QQU

Asymetric subunit of E. coli DNA gyrase bound to a linear part of a DNA minicircle

Functional Information from GO Data
ChainGOidnamespacecontents
C0000166molecular_functionnucleotide binding
C0003677molecular_functionDNA binding
C0003916molecular_functionDNA topoisomerase activity
C0003918molecular_functionDNA topoisomerase type II (double strand cut, ATP-hydrolyzing) activity
C0005515molecular_functionprotein binding
C0005524molecular_functionATP binding
C0005694cellular_componentchromosome
C0005737cellular_componentcytoplasm
C0005829cellular_componentcytosol
C0006259biological_processDNA metabolic process
C0006261biological_processDNA-templated DNA replication
C0006265biological_processDNA topological change
C0006351biological_processDNA-templated transcription
C0008094molecular_functionATP-dependent activity, acting on DNA
C0009330cellular_componentDNA topoisomerase type II (double strand cut, ATP-hydrolyzing) complex
C0009410biological_processresponse to xenobiotic stimulus
C0016020cellular_componentmembrane
C0016853molecular_functionisomerase activity
C0034335molecular_functionDNA negative supercoiling activity
C0042802molecular_functionidentical protein binding
C0046677biological_processresponse to antibiotic
C0051276biological_processchromosome organization
C2000104biological_processnegative regulation of DNA-templated DNA replication
D0000166molecular_functionnucleotide binding
D0003677molecular_functionDNA binding
D0003916molecular_functionDNA topoisomerase activity
D0003918molecular_functionDNA topoisomerase type II (double strand cut, ATP-hydrolyzing) activity
D0005515molecular_functionprotein binding
D0005524molecular_functionATP binding
D0005694cellular_componentchromosome
D0005737cellular_componentcytoplasm
D0005829cellular_componentcytosol
D0006261biological_processDNA-templated DNA replication
D0006265biological_processDNA topological change
D0006351biological_processDNA-templated transcription
D0008094molecular_functionATP-dependent activity, acting on DNA
D0009330cellular_componentDNA topoisomerase type II (double strand cut, ATP-hydrolyzing) complex
D0009410biological_processresponse to xenobiotic stimulus
D0016853molecular_functionisomerase activity
D0034335molecular_functionDNA negative supercoiling activity
D0046677biological_processresponse to antibiotic
D0046872molecular_functionmetal ion binding
D0051276biological_processchromosome organization
Functional Information from PROSITE/UniProt
site_idPS00177
Number of Residues9
DetailsTOPOISOMERASE_II DNA topoisomerase II signature. LVEGDSAGG
ChainResidueDetails
DLEU422-GLY430

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsActive site: {"description":"O-(5'-phospho-DNA)-tyrosine intermediate","evidences":[{"source":"HAMAP-Rule","id":"MF_01897","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"3031051","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues115
DetailsDomain: {"description":"Toprim","evidences":[{"source":"HAMAP-Rule","id":"MF_01898","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues171
DetailsRegion: {"description":"Transducer domain","evidences":[{"source":"PubMed","id":"10734094","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"1646964","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues1
DetailsActive site: {"description":"Proton acceptor (ATPase activity)","evidences":[{"source":"PubMed","id":"10734094","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"8248233","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"10734094","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"25202966","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"25849408","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues1
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"25849408","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"10734094","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"25849408","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues3
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01898","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"12051843","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"18642932","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues1
DetailsSite: {"description":"Transition state stabilizer","evidences":[{"source":"PubMed","id":"9657678","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues2
DetailsSite: {"description":"Interaction with DNA","evidences":[{"source":"HAMAP-Rule","id":"MF_01898","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idMCSA1
Number of Residues3
DetailsM-CSA 745
ChainResidueDetails

247536

PDB entries from 2026-01-14

PDB statisticsPDBj update infoContact PDBjnumon