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4G0W

Human topoisomerase iibeta in complex with DNA and ametantrone

Functional Information from GO Data
ChainGOidnamespacecontents
A0003677molecular_functionDNA binding
A0003918molecular_functionDNA topoisomerase type II (double strand cut, ATP-hydrolyzing) activity
A0005524molecular_functionATP binding
A0006259biological_processDNA metabolic process
A0006265biological_processDNA topological change
B0003677molecular_functionDNA binding
B0003918molecular_functionDNA topoisomerase type II (double strand cut, ATP-hydrolyzing) activity
B0005524molecular_functionATP binding
B0006259biological_processDNA metabolic process
B0006265biological_processDNA topological change
Functional Information from PDB Data
site_id1
Number of Residues
Details
ChainResidue

site_idAC1
Number of Residues2
DetailsBINDING SITE FOR RESIDUE MG A 1301
ChainResidue
AASP557
AASP559

site_idAC2
Number of Residues2
DetailsBINDING SITE FOR RESIDUE MG A 1302
ChainResidue
AASN867
AGLY868

site_idAC3
Number of Residues2
DetailsBINDING SITE FOR RESIDUE MG B 1301
ChainResidue
BASP557
BASP559

site_idAC4
Number of Residues1
DetailsBINDING SITE FOR RESIDUE MG B 1302
ChainResidue
BASN867

site_idAC5
Number of Residues14
DetailsBINDING SITE FOR RESIDUE AKE D 101
ChainResidue
BLYS505
BLEU507
BASN520
BGLU522
BGLN778
BMET782
DDA12
DDG13
DDC14
EDG7
EDC8
FDT9
BARG503
BGLY504

site_idAC6
Number of Residues1
DetailsBINDING SITE FOR RESIDUE MG D 102
ChainResidue
DDG18

site_idAC7
Number of Residues13
DetailsBINDING SITE FOR RESIDUE AKE F 101
ChainResidue
AARG503
ALYS505
AILE506
AASN520
AGLU522
AGLN778
AMET782
CDG7
CDC8
DDT9
FDA12
FDG13
FDC14

site_idAC8
Number of Residues1
DetailsBINDING SITE FOR RESIDUE MG F 102
ChainResidue
FDG17

Functional Information from PROSITE/UniProt
site_idPS00177
Number of Residues9
DetailsTOPOISOMERASE_II DNA topoisomerase II signature. LTEGDSAKS
ChainResidueDetails
ALEU475-SER483

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 Residues8
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)","evidences":[{"source":"PubMed","id":"28112733","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

239149

PDB entries from 2025-07-23

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