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5GWK

Human topoisomerase IIalpha in complex with DNA and etoposide

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_idAC1
Number of Residues2
Detailsbinding site for residue MG A 1301
ChainResidue
AASP541
AASP543

site_idAC2
Number of Residues3
Detailsbinding site for residue MG A 1302
ChainResidue
AASN851
AGLU854
AARG929

site_idAC3
Number of Residues2
Detailsbinding site for residue MG B 1301
ChainResidue
BASP541
BASP543

site_idAC4
Number of Residues2
Detailsbinding site for residue MG B 1302
ChainResidue
BASN851
BARG929

site_idAC5
Number of Residues1
Detailsbinding site for residue MG D 101
ChainResidue
DDG17

site_idAC6
Number of Residues9
Detailsbinding site for residue EVP D 102
ChainResidue
BGLY462
BASP463
BARG487
BMET766
DDA12
DDG13
EDC8
FDT9
FDG10

site_idAC7
Number of Residues1
Detailsbinding site for residue MG F 101
ChainResidue
FDG17

site_idAC8
Number of Residues10
Detailsbinding site for residue EVP F 102
ChainResidue
AGLY462
AASP463
AARG487
AMET762
AMET766
CDC8
DDT9
DDG10
FDA12
FDG13

Functional Information from PROSITE/UniProt
site_idPS00177
Number of Residues9
DetailsTOPOISOMERASE_II DNA topoisomerase II signature. LTEGDSAKT
ChainResidueDetails
ALEU459-THR467

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: O-(5'-phospho-DNA)-tyrosine intermediate => ECO:0000255|PROSITE-ProRule:PRU01384
ChainResidueDetails
ATYR805
BTYR805

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00995
ChainResidueDetails
AGLU461
BGLU461

site_idSWS_FT_FI3
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:22841979
ChainResidueDetails
AASP541
AASP543
BASP541
BASP543

site_idSWS_FT_FI4
Number of Residues2
DetailsSITE: Interaction with DNA => ECO:0000255|PROSITE-ProRule:PRU00995
ChainResidueDetails
ALYS489
BLYS489

site_idSWS_FT_FI5
Number of Residues14
DetailsSITE: Interaction with DNA => ECO:0000269|PubMed:22841979
ChainResidueDetails
AASN492
BLYS662
BLYS723
BTYR757
BSER763
BTRP931
AARG661
ALYS662
ALYS723
ATYR757
ASER763
ATRP931
BASN492
BARG661

site_idSWS_FT_FI6
Number of Residues2
DetailsSITE: Transition state stabilizer => ECO:0000250|UniProtKB:P06786
ChainResidueDetails
AARG804
BARG804

site_idSWS_FT_FI7
Number of Residues2
DetailsSITE: Important for DNA bending; intercalates between base pairs of target DNA => ECO:0000250|UniProtKB:P06786
ChainResidueDetails
AILE856
BILE856

site_idSWS_FT_FI8
Number of Residues2
DetailsMOD_RES: Phosphoserine; by CK1 => ECO:0000269|PubMed:19043076, ECO:0000269|Ref.11, ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER1106
BSER1106

site_idSWS_FT_FI9
Number of Residues26
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:28112733
ChainResidueDetails
ALYS440
ALYS625
ALYS632
ALYS655
ALYS1114
BLYS440
BLYS466
BLYS480
BLYS529
BLYS584
BLYS599
BLYS614
BLYS622
BLYS625
BLYS632
BLYS655
BLYS1114
ALYS466
ALYS480
ALYS529
ALYS584
ALYS599
ALYS614
ALYS622

site_idSWS_FT_FI10
Number of Residues8
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:25772364, ECO:0007744|PubMed:28112733
ChainResidueDetails
ALYS639
ALYS662
ALYS676
ALYS1075
BLYS639
BLYS662
BLYS676
BLYS1075

237992

PDB entries from 2025-06-25

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