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7YQ8

Cryo-EM structure of human topoisomerase II beta in complex with DNA and etoposide

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0000712biological_processresolution of meiotic recombination intermediates
A0000792cellular_componentheterochromatin
A0000819biological_processsister chromatid segregation
A0003677molecular_functionDNA binding
A0003682molecular_functionchromatin binding
A0003916molecular_functionDNA topoisomerase activity
A0003918molecular_functionDNA topoisomerase type II (double strand cut, ATP-hydrolyzing) activity
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0005634cellular_componentnucleus
A0005654cellular_componentnucleoplasm
A0005730cellular_componentnucleolus
A0005829cellular_componentcytosol
A0006259biological_processDNA metabolic process
A0006265biological_processDNA topological change
A0016853molecular_functionisomerase activity
A0030183biological_processB cell differentiation
A0043021molecular_functionribonucleoprotein complex binding
A0045870biological_processpositive regulation of single stranded viral RNA replication via double stranded DNA intermediate
A0046872molecular_functionmetal ion binding
A0070301biological_processcellular response to hydrogen peroxide
A0071318biological_processcellular response to ATP
A0090398biological_processcellular senescence
A1990904cellular_componentribonucleoprotein complex
A2001034biological_processpositive regulation of double-strand break repair via nonhomologous end joining
B0000166molecular_functionnucleotide binding
B0000712biological_processresolution of meiotic recombination intermediates
B0000792cellular_componentheterochromatin
B0000819biological_processsister chromatid segregation
B0003677molecular_functionDNA binding
B0003682molecular_functionchromatin binding
B0003916molecular_functionDNA topoisomerase activity
B0003918molecular_functionDNA topoisomerase type II (double strand cut, ATP-hydrolyzing) activity
B0005515molecular_functionprotein binding
B0005524molecular_functionATP binding
B0005634cellular_componentnucleus
B0005654cellular_componentnucleoplasm
B0005730cellular_componentnucleolus
B0005829cellular_componentcytosol
B0006259biological_processDNA metabolic process
B0006265biological_processDNA topological change
B0016853molecular_functionisomerase activity
B0030183biological_processB cell differentiation
B0043021molecular_functionribonucleoprotein complex binding
B0045870biological_processpositive regulation of single stranded viral RNA replication via double stranded DNA intermediate
B0046872molecular_functionmetal ion binding
B0070301biological_processcellular response to hydrogen peroxide
B0071318biological_processcellular response to ATP
B0090398biological_processcellular senescence
B1990904cellular_componentribonucleoprotein complex
B2001034biological_processpositive regulation of double-strand break repair via nonhomologous end joining
Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues22
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. VGGGNGALTWvTlfdqnn............AAKK
ChainResidueDetails
AVAL13-LYS34

site_idPS00177
Number of Residues9
DetailsTOPOISOMERASE_II DNA topoisomerase II signature. LTEGDSAKS
ChainResidueDetails
ALEU480-SER488

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues234
DetailsDomain: {"description":"Toprim","evidences":[{"source":"PROSITE-ProRule","id":"PRU00995","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues18
DetailsRegion: {"description":"Interaction with DNA"}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues20
DetailsMotif: {"description":"Nuclear export signal"}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues2
DetailsActive site: {"description":"O-(5'-phospho-DNA)-tyrosine intermediate","evidences":[{"source":"PROSITE-ProRule","id":"PRU01384","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"21778401","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00995","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00995","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"21778401","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues12
DetailsSite: {"description":"Interaction with DNA"}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues2
DetailsSite: {"description":"Interaction with DNA","evidences":[{"source":"PROSITE-ProRule","id":"PRU00995","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues2
DetailsSite: {"description":"Transition state stabilizer"}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues2
DetailsSite: {"description":"Important for DNA bending; intercalates between base pairs of target DNA"}
ChainResidueDetails

site_idSWS_FT_FI11
Number of Residues14
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)","evidences":[{"source":"PubMed","id":"28112733","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI12
Number of Residues4
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)","evidences":[{"source":"PubMed","id":"25772364","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"28112733","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

247536

PDB entries from 2026-01-14

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