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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 Residues2
DetailsACT_SITE: O-(5'-phospho-DNA)-tyrosine intermediate => ECO:0000255|PROSITE-ProRule:PRU01384, ECO:0000269|PubMed:21778401
ChainResidueDetails
ATYR821
BTYR821

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00995
ChainResidueDetails
AGLU477
BGLU477

site_idSWS_FT_FI3
Number of Residues4
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00995, ECO:0000269|PubMed:21778401
ChainResidueDetails
AASP557
AASP559
BASP557
BASP559

site_idSWS_FT_FI4
Number of Residues12
DetailsSITE: Interaction with DNA
ChainResidueDetails
ALYS505
AASN508
AARG677
ALYS678
ALYS739
ATRP947
BLYS505
BASN508
BARG677
BLYS678
BLYS739
BTRP947

site_idSWS_FT_FI5
Number of Residues2
DetailsSITE: Interaction with DNA => ECO:0000255|PROSITE-ProRule:PRU00995
ChainResidueDetails
ATYR773
BTYR773

site_idSWS_FT_FI6
Number of Residues2
DetailsSITE: Transition state stabilizer
ChainResidueDetails
AARG820
BARG820

site_idSWS_FT_FI7
Number of Residues2
DetailsSITE: Important for DNA bending; intercalates between base pairs of target DNA
ChainResidueDetails
BILE872
AILE872

site_idSWS_FT_FI8
Number of Residues14
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:28112733
ChainResidueDetails
ALYS595
ALYS630
ALYS641
ALYS671
ALYS707
ALYS1087
BLYS595
BLYS630
BLYS641
BLYS671
BLYS707
BLYS1087

site_idSWS_FT_FI9
Number of Residues4
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:25772364, ECO:0007744|PubMed:28112733
ChainResidueDetails
ALYS600
ALYS638
BLYS600
BLYS638

218500

건을2024-04-17부터공개중

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