Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

6ZY7

Cryo-EM structure of the entire Human topoisomerase II alpha in State 1

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
A	0000228	cellular_component	nuclear chromosome
A	0000287	molecular_function	magnesium ion binding
A	0000712	biological_process	resolution of meiotic recombination intermediates
A	0000775	cellular_component	chromosome, centromeric region
A	0000793	cellular_component	condensed chromosome
A	0000819	biological_process	sister chromatid segregation
A	0003677	molecular_function	DNA binding
A	0003682	molecular_function	chromatin binding
A	0003723	molecular_function	RNA binding
A	0003916	molecular_function	DNA topoisomerase activity
A	0003918	molecular_function	DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) activity
A	0005080	molecular_function	protein kinase C binding
A	0005515	molecular_function	protein binding
A	0005524	molecular_function	ATP binding
A	0005634	cellular_component	nucleus
A	0005654	cellular_component	nucleoplasm
A	0005730	cellular_component	nucleolus
A	0005737	cellular_component	cytoplasm
A	0005814	cellular_component	centriole
A	0006259	biological_process	DNA metabolic process
A	0006265	biological_process	DNA topological change
A	0006325	biological_process	chromatin organization
A	0006974	biological_process	DNA damage response
A	0007059	biological_process	chromosome segregation
A	0007143	biological_process	female meiotic nuclear division
A	0008094	molecular_function	ATP-dependent activity, acting on DNA
A	0008301	molecular_function	DNA binding, bending
A	0009330	cellular_component	DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) complex
A	0016853	molecular_function	isomerase activity
A	0030263	biological_process	apoptotic chromosome condensation
A	0032991	cellular_component	protein-containing complex
A	0042752	biological_process	regulation of circadian rhythm
A	0042803	molecular_function	protein homodimerization activity
A	0043065	biological_process	positive regulation of apoptotic process
A	0043130	molecular_function	ubiquitin binding
A	0045870	biological_process	positive regulation of single stranded viral RNA replication via double stranded DNA intermediate
A	0046872	molecular_function	metal ion binding
A	0046982	molecular_function	protein heterodimerization activity
A	0048511	biological_process	rhythmic process
A	1990904	cellular_component	ribonucleoprotein complex
B	0000166	molecular_function	nucleotide binding
B	0000228	cellular_component	nuclear chromosome
B	0000287	molecular_function	magnesium ion binding
B	0000712	biological_process	resolution of meiotic recombination intermediates
B	0000775	cellular_component	chromosome, centromeric region
B	0000793	cellular_component	condensed chromosome
B	0000819	biological_process	sister chromatid segregation
B	0003677	molecular_function	DNA binding
B	0003682	molecular_function	chromatin binding
B	0003723	molecular_function	RNA binding
B	0003916	molecular_function	DNA topoisomerase activity
B	0003918	molecular_function	DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) activity
B	0005080	molecular_function	protein kinase C binding
B	0005515	molecular_function	protein binding
B	0005524	molecular_function	ATP binding
B	0005634	cellular_component	nucleus
B	0005654	cellular_component	nucleoplasm
B	0005730	cellular_component	nucleolus
B	0005737	cellular_component	cytoplasm
B	0005814	cellular_component	centriole
B	0006259	biological_process	DNA metabolic process
B	0006265	biological_process	DNA topological change
B	0006325	biological_process	chromatin organization
B	0006974	biological_process	DNA damage response
B	0007059	biological_process	chromosome segregation
B	0007143	biological_process	female meiotic nuclear division
B	0008094	molecular_function	ATP-dependent activity, acting on DNA
B	0008301	molecular_function	DNA binding, bending
B	0009330	cellular_component	DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) complex
B	0016853	molecular_function	isomerase activity
B	0030263	biological_process	apoptotic chromosome condensation
B	0032991	cellular_component	protein-containing complex
B	0042752	biological_process	regulation of circadian rhythm
B	0042803	molecular_function	protein homodimerization activity
B	0043065	biological_process	positive regulation of apoptotic process
B	0043130	molecular_function	ubiquitin binding
B	0045870	biological_process	positive regulation of single stranded viral RNA replication via double stranded DNA intermediate
B	0046872	molecular_function	metal ion binding
B	0046982	molecular_function	protein heterodimerization activity
B	0048511	biological_process	rhythmic process
B	1990904	cellular_component	ribonucleoprotein complex

Functional Information from PROSITE/UniProt

site_id	PS00177
Number of Residues	9
Details	TOPOISOMERASE_II DNA topoisomerase II signature. LTEGDSAKT

Chain	Residue	Details
B	LEU459-THR467

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	234
Details	Domain: {"description":"Toprim","evidences":[{"source":"PROSITE-ProRule","id":"PRU00995","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	4
Details	Region: {"description":"Interaction with DNA","evidences":[{"source":"PubMed","id":"23022727","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	18
Details	Region: {"description":"Interaction with DNA","evidences":[{"source":"PubMed","id":"22841979","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	20
Details	Motif: {"description":"Nuclear export signal"}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	2
Details	Active site: {"description":"O-(5'-phospho-DNA)-tyrosine intermediate","evidences":[{"source":"PROSITE-ProRule","id":"PRU01384","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	22
Details	Binding site: {"evidences":[{"source":"PubMed","id":"16100112","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"25202966","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"PubMed","id":"16100112","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"25202966","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00995","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI9
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"PubMed","id":"22841979","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI10
Number of Residues	2
Details	Site: {"description":"Interaction with DNA","evidences":[{"source":"PROSITE-ProRule","id":"PRU00995","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI11
Number of Residues	14
Details	Site: {"description":"Interaction with DNA","evidences":[{"source":"PubMed","id":"22841979","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI12
Number of Residues	2
Details	Site: {"description":"Transition state stabilizer","evidences":[{"source":"UniProtKB","id":"P06786","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI13
Number of Residues	2
Details	Site: {"description":"Important for DNA bending; intercalates between base pairs of target DNA","evidences":[{"source":"UniProtKB","id":"P06786","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI14
Number of Residues	4
Details	Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"20068231","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI15
Number of Residues	2
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"16964243","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"17081983","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"18669648","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"18691976","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"20068231","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"21406692","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI16
Number of Residues	44
Details	Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)","evidences":[{"source":"PubMed","id":"28112733","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI17
Number of Residues	10
Details	Cross-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"}]}

Chain

Residue

Details

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)