eF-site ID 4g0w-ABCDEF PDB Code 4g0w Chain A, B, C, D, E, F click to enlarge Title Human topoisomerase iibeta in complex with DNA and ametantrone Classification ISOMERASE/DNA/ISOMERASE INHIBITOR Compound DNA topoisomerase 2-beta Source Homo sapiens (Human) (4G0W) Sequence A:  KGIPKLDDANDAGGKHSLECTLILTEGDSAKSLAVSGLGV IGRDRYGVFPLRGKILNVREASHKQIMENAEINNIIKIVG LQYKKSYDDAESLKTLRYGKIMIMTDQDQDGSHIKGLLIN FIHHNWPSLLKHGFLEEFITADMERHRILFRYAGPEDDAA ITLAFSKKKIDDRKEWLTNFMEDRRQRRLHGLKHLTYNDF INKELILFSNSDNERSIPSLVDGFKPGQRKVLFTCFKRND KREVKVAQLAGSVAEMSAYHHGEQALMMTIVNLAQNFVGS NNINLLQPIGQFGTRLHGGKDAASPRYIFTMLSTLARLLF PAVDDNLLKFLYDDNQRVEPEWYIPIIPMVLINGAEGIGT GWACKLPNYDAREIVNNVRRMLDGLDPHPMLPNYKNFKGT IQELGQNQYAVSGEIFVVDRNTVEITELPVRTWTQVYKEQ VLEPMLNGTDKTPALISDYKEYHTDTTVKFVVKMTEEKLA QAEAAGLHKVFKLQTTLTCNSMVLFDHMGCLKKYETVQDI LKEFFDLRLSYYGLRKEWLVGMLGAESTKLNNQARFILEK IQGKITIENRSKKDLIQMLVQRGYESDPVKAWKEAQEGPD FNYILNMSLWSLTKEKVEELIKQRDAKGREVNDLKRKSPS DLWKEDLAAFVEELDKVESQERED B:  SKIKGIPKLDDANDAGGKHSLECTLILTEGDSAKSLAVSG LGVIGRDRYGVFPLRGKILNVREASHKQIMENAEINNIIK IVGLQYKKSYDDAESLKTLRYGKIMIMTDQDQDGSHIKGL LINFIHHNWPSLLKHGFLEEFITPFADMERHRILFRYAGP EDDAAITLAFSKKKIDDRKEWLTNFMEDRRQRRLHGTKHL TYNDFINKELILFSNSDNERSIPSLVDGFKPGQRKVLFTC FKRNDKREVKVAQLAGSVAEMSAYHHGEQALMMTIVNLAQ NFVGSNNINLLQPIGQFGTRLHGGKDAASPRYIFTMLSTL ARLLFPAVDDNLLKFLYDDNQRVEPEWYIPIIPMVLINGA EGIGTGWACKLPNYDAREIVNNVRRMLDGLDPHPMLPNYK NFKGTIQELGQNQYAVSGEIFVVDRNTVEITELPVRTWTQ VYKEQVLEPMLNGPALISDYKEYHTDTTVKFVVKMTEEKL AQAEAAGLHKVFKLQTTLTCNSMVLFDHMGCLKKYETVQD ILKEFFDLRLSYYGLRKEWLVGMLGAESTKLNNQARFILE KIQGKITIENRSKKDLIQMLVQRGYESDPVKAWKEAQGPD FNYILNMSLWSLTKEKVEELIKQRDAKGREVNDLKRKSPS DLWKEDLAAFVEELDKVESQERED C:  AGCCGAGC D:  TGCAGCTCGGCT E:  AGCCGAGC F:  TGCAGCTCGGCT Description Functional site 1) chain A residue 557 type sequence D description BINDING SITE FOR RESIDUE MG A 1301 source : AC1 2) chain A residue 559 type sequence D description BINDING SITE FOR RESIDUE MG A 1301 source : AC1 3) chain A residue 867 type sequence N description BINDING SITE FOR RESIDUE MG A 1302 source : AC2 4) chain A residue 868 type sequence G description BINDING SITE FOR RESIDUE MG A 1302 source : AC2 5) chain B residue 557 type sequence D description BINDING SITE FOR RESIDUE MG B 1301 source : AC3 6) chain B residue 559 type sequence D description BINDING SITE FOR RESIDUE MG B 1301 source : AC3 7) chain B residue 867 type sequence N description BINDING SITE FOR RESIDUE MG B 1302 source : AC4 8) chain B residue 503 type sequence R description BINDING SITE FOR RESIDUE AKE D 101 source : AC5 9) chain B residue 504 type sequence G description BINDING SITE FOR RESIDUE AKE D 101 source : AC5 10) chain B residue 505 type sequence K description BINDING SITE FOR RESIDUE AKE D 101 source : AC5 11) chain B residue 507 type sequence L description BINDING SITE FOR RESIDUE AKE D 101 source : AC5 12) chain B residue 520 type sequence N description BINDING SITE FOR RESIDUE AKE D 101 source : AC5 13) chain B residue 522 type sequence E description BINDING SITE FOR RESIDUE AKE D 101 source : AC5 14) chain B residue 778 type sequence Q description BINDING SITE FOR RESIDUE AKE D 101 source : AC5 15) chain B residue 782 type sequence M description BINDING SITE FOR RESIDUE AKE D 101 source : AC5 16) chain D residue 12 type sequence A description BINDING SITE FOR RESIDUE AKE D 101 source : AC5 17) chain D residue 13 type sequence G description BINDING SITE FOR RESIDUE AKE D 101 source : AC5 18) chain D residue 14 type sequence C description BINDING SITE FOR RESIDUE AKE D 101 source : AC5 19) chain E residue 7 type sequence G description BINDING SITE FOR RESIDUE AKE D 101 source : AC5 20) chain E residue 8 type sequence C description BINDING SITE FOR RESIDUE AKE D 101 source : AC5 21) chain F residue 9 type sequence T description BINDING SITE FOR RESIDUE AKE D 101 source : AC5 22) chain D residue 18 type sequence G description BINDING SITE FOR RESIDUE MG D 102 source : AC6 23) chain A residue 503 type sequence R description BINDING SITE FOR RESIDUE AKE F 101 source : AC7 24) chain A residue 505 type sequence K description BINDING SITE FOR RESIDUE AKE F 101 source : AC7 25) chain A residue 506 type sequence I description BINDING SITE FOR RESIDUE AKE F 101 source : AC7 26) chain A residue 520 type sequence N description BINDING SITE FOR RESIDUE AKE F 101 source : AC7 27) chain A residue 522 type sequence E description BINDING SITE FOR RESIDUE AKE F 101 source : AC7 28) chain A residue 778 type sequence Q description BINDING SITE FOR RESIDUE AKE F 101 source : AC7 29) chain A residue 782 type sequence M description BINDING SITE FOR RESIDUE AKE F 101 source : AC7 30) chain C residue 7 type sequence G description BINDING SITE FOR RESIDUE AKE F 101 source : AC7 31) chain C residue 8 type sequence C description BINDING SITE FOR RESIDUE AKE F 101 source : AC7 32) chain D residue 9 type sequence T description BINDING SITE FOR RESIDUE AKE F 101 source : AC7 33) chain F residue 12 type sequence A description BINDING SITE FOR RESIDUE AKE F 101 source : AC7 34) chain F residue 13 type sequence G description BINDING SITE FOR RESIDUE AKE F 101 source : AC7 35) chain F residue 14 type sequence C description BINDING SITE FOR RESIDUE AKE F 101 source : AC7 36) chain F residue 17 type sequence G description BINDING SITE FOR RESIDUE MG F 102 source : AC8 37) chain A residue 477 type BINDING sequence E description BINDING => ECO:0000255|PROSITE-ProRule:PRU00995 source Swiss-Prot : SWS_FT_FI2 38) chain B residue 477 type BINDING sequence E description BINDING => ECO:0000255|PROSITE-ProRule:PRU00995 source Swiss-Prot : SWS_FT_FI2 39) chain A residue 557 type BINDING sequence D description BINDING => ECO:0000255|PROSITE-ProRule:PRU00995, ECO:0000269|PubMed:21778401 source Swiss-Prot : SWS_FT_FI3 40) chain A residue 559 type BINDING sequence D description BINDING => ECO:0000255|PROSITE-ProRule:PRU00995, ECO:0000269|PubMed:21778401 source Swiss-Prot : SWS_FT_FI3 41) chain B residue 557 type BINDING sequence D description BINDING => ECO:0000255|PROSITE-ProRule:PRU00995, ECO:0000269|PubMed:21778401 source Swiss-Prot : SWS_FT_FI3 42) chain B residue 559 type BINDING sequence D description BINDING => ECO:0000255|PROSITE-ProRule:PRU00995, ECO:0000269|PubMed:21778401 source Swiss-Prot : SWS_FT_FI3 43) chain A residue 505 type SITE sequence K description Interaction with DNA source Swiss-Prot : SWS_FT_FI4 44) chain B residue 678 type SITE sequence K description Interaction with DNA source Swiss-Prot : SWS_FT_FI4 45) chain B residue 739 type SITE sequence K description Interaction with DNA source Swiss-Prot : SWS_FT_FI4 46) chain B residue 947 type SITE sequence W description Interaction with DNA source Swiss-Prot : SWS_FT_FI4 47) chain A residue 508 type SITE sequence N description Interaction with DNA source Swiss-Prot : SWS_FT_FI4 48) chain A residue 677 type SITE sequence R description Interaction with DNA source Swiss-Prot : SWS_FT_FI4 49) chain A residue 678 type SITE sequence K description Interaction with DNA source Swiss-Prot : SWS_FT_FI4 50) chain A residue 739 type SITE sequence K description Interaction with DNA source Swiss-Prot : SWS_FT_FI4 51) chain A residue 947 type SITE sequence W description Interaction with DNA source Swiss-Prot : SWS_FT_FI4 52) chain B residue 505 type SITE sequence K description Interaction with DNA source Swiss-Prot : SWS_FT_FI4 53) chain B residue 508 type SITE sequence N description Interaction with DNA source Swiss-Prot : SWS_FT_FI4 54) chain B residue 677 type SITE sequence R description Interaction with DNA source Swiss-Prot : SWS_FT_FI4 55) chain A residue 773 type SITE sequence Y description Interaction with DNA => ECO:0000255|PROSITE-ProRule:PRU00995 source Swiss-Prot : SWS_FT_FI5 56) chain B residue 773 type SITE sequence Y description Interaction with DNA => ECO:0000255|PROSITE-ProRule:PRU00995 source Swiss-Prot : SWS_FT_FI5 57) chain A residue 820 type SITE sequence R description Transition state stabilizer source Swiss-Prot : SWS_FT_FI6 58) chain B residue 820 type SITE sequence R description Transition state stabilizer source Swiss-Prot : SWS_FT_FI6 59) chain A residue 872 type SITE sequence I description Important for DNA bending; intercalates between base pairs of target DNA source Swiss-Prot : SWS_FT_FI7 60) chain B residue 872 type SITE sequence I description Important for DNA bending; intercalates between base pairs of target DNA source Swiss-Prot : SWS_FT_FI7 61) chain A residue 475-483 type prosite sequence LTEGDSAKS description TOPOISOMERASE_II DNA topoisomerase II signature. LTEGDSAKS source prosite : PS00177 62) chain B residue 671 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:28112733 source Swiss-Prot : SWS_FT_FI8 63) chain B residue 707 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:28112733 source Swiss-Prot : SWS_FT_FI8 64) chain B residue 1087 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:28112733 source Swiss-Prot : SWS_FT_FI8 65) chain A residue 671 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:28112733 source Swiss-Prot : SWS_FT_FI8 66) chain A residue 707 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:28112733 source Swiss-Prot : SWS_FT_FI8 67) chain A residue 1087 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:28112733 source Swiss-Prot : SWS_FT_FI8 68) chain A residue 821 type ACT_SITE sequence Y description O-(5'-phospho-DNA)-tyrosine intermediate => ECO:0000255|PROSITE-ProRule:PRU01384, ECO:0000269|PubMed:21778401 source Swiss-Prot : SWS_FT_FI1 69) chain B residue 821 type ACT_SITE sequence Y description O-(5'-phospho-DNA)-tyrosine intermediate => ECO:0000255|PROSITE-ProRule:PRU01384, ECO:0000269|PubMed:21778401 source Swiss-Prot : SWS_FT_FI1

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