Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1MX0

Structure of topoisomerase subunit

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003676	molecular_function	nucleic acid binding
A	0003677	molecular_function	DNA binding
A	0003918	molecular_function	DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) activity
A	0005524	molecular_function	ATP binding
A	0006265	biological_process	DNA topological change
B	0003676	molecular_function	nucleic acid binding
B	0003677	molecular_function	DNA binding
B	0003918	molecular_function	DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) activity
B	0005524	molecular_function	ATP binding
B	0006265	biological_process	DNA topological change
C	0003676	molecular_function	nucleic acid binding
C	0003677	molecular_function	DNA binding
C	0003918	molecular_function	DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) activity
C	0005524	molecular_function	ATP binding
C	0006265	biological_process	DNA topological change
D	0003676	molecular_function	nucleic acid binding
D	0003677	molecular_function	DNA binding
D	0003918	molecular_function	DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) activity
D	0005524	molecular_function	ATP binding
D	0006265	biological_process	DNA topological change
E	0003676	molecular_function	nucleic acid binding
E	0003677	molecular_function	DNA binding
E	0003918	molecular_function	DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) activity
E	0005524	molecular_function	ATP binding
E	0006265	biological_process	DNA topological change
F	0003676	molecular_function	nucleic acid binding
F	0003677	molecular_function	DNA binding
F	0003918	molecular_function	DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) activity
F	0005524	molecular_function	ATP binding
F	0006265	biological_process	DNA topological change

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MG A 501

Chain	Residue
A	ASN42
A	ANP900
A	HOH913
A	HOH915

site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MG B 501

Chain	Residue
B	ASN42
B	ANP910
B	HOH949
B	HOH985

site_id	AC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MG C 501

Chain	Residue
C	ANP920
C	HOH948
C	HOH1048
C	ASN42

site_id	AC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MG D 501

Chain	Residue
D	ASN42
D	ANP930
D	HOH932
D	HOH1045

site_id	AC5
Number of Residues	3
Details	BINDING SITE FOR RESIDUE MG E 501

Chain	Residue
E	ASN42
E	ANP940
E	HOH976

site_id	AC6
Number of Residues	3
Details	BINDING SITE FOR RESIDUE MG F 501

Chain	Residue
F	ASN42
F	ANP950
F	HOH982

site_id	AC7
Number of Residues	4
Details	BINDING SITE FOR RESIDUE NA D 901

Chain	Residue
D	VAL259
D	PHE262
D	ILE265
D	HOH954

site_id	AC8
Number of Residues	25
Details	BINDING SITE FOR RESIDUE ANP A 900

Chain	Residue
A	GLU38
A	ASN42
A	ALA46
A	ASP76
A	GLY80
A	ILE81
A	ALA89
A	SER96
A	SER97
A	LYS98
A	GLY106
A	MSE107
A	TYR108
A	GLY109
A	LEU110
A	GLY111
A	VAL112
A	LYS113
A	LYS427
A	MG501
A	HOH905
A	HOH912
A	HOH915
A	HOH969
B	PHE7

site_id	AC9
Number of Residues	25
Details	BINDING SITE FOR RESIDUE ANP B 910

Chain	Residue
A	PHE7
B	ASN42
B	ALA46
B	ASP76
B	GLY80
B	ILE81
B	ALA89
B	SER96
B	SER97
B	LYS98
B	GLY106
B	MSE107
B	TYR108
B	GLY109
B	LEU110
B	GLY111
B	VAL112
B	LYS113
B	THR170
B	LYS427
B	MG501
B	HOH911
B	HOH922
B	HOH978
B	HOH985

site_id	BC1
Number of Residues	28
Details	BINDING SITE FOR RESIDUE ANP C 920

Chain	Residue
C	HOH948
C	HOH980
C	HOH982
C	HOH1048
D	PHE7
C	GLU38
C	ASN42
C	ALA46
C	ASP76
C	ILE81
C	ALA89
C	PHE90
C	SER96
C	SER97
C	LYS98
C	GLY106
C	MSE107
C	TYR108
C	GLY109
C	LEU110
C	GLY111
C	VAL112
C	LYS113
C	THR170
C	LYS427
C	MG501
C	HOH924
C	HOH931

site_id	BC2
Number of Residues	26
Details	BINDING SITE FOR RESIDUE ANP D 930

Chain	Residue
C	PHE7
D	GLU38
D	ASN42
D	ALA46
D	ASP76
D	ILE81
D	ALA89
D	SER96
D	SER97
D	LYS98
D	GLY106
D	MSE107
D	TYR108
D	GLY109
D	LEU110
D	GLY111
D	VAL112
D	LYS113
D	LYS427
D	MG501
D	HOH932
D	HOH934
D	HOH938
D	HOH940
D	HOH943
D	HOH1045

site_id	BC3
Number of Residues	26
Details	BINDING SITE FOR RESIDUE ANP E 940

Chain	Residue
E	GLU38
E	ASN42
E	ALA46
E	ASP76
E	ILE81
E	ALA89
E	SER96
E	SER97
E	LYS98
E	GLY106
E	MSE107
E	TYR108
E	GLY109
E	LEU110
E	GLY111
E	VAL112
E	LYS113
E	THR170
E	LYS427
E	MG501
E	HOH941
E	HOH943
E	HOH949
E	HOH961
E	HOH976
F	PHE7

site_id	BC4
Number of Residues	27
Details	BINDING SITE FOR RESIDUE ANP F 950

Chain	Residue
E	PHE7
F	ASN42
F	SER43
F	ALA46
F	ASP76
F	GLY80
F	ILE81
F	ALA89
F	TYR95
F	SER96
F	SER97
F	LYS98
F	GLY106
F	MSE107
F	TYR108
F	GLY109
F	LEU110
F	GLY111
F	VAL112
F	LYS113
F	LYS427
F	MG501
F	HOH951
F	HOH979
F	HOH982
F	HOH998
F	HOH1017

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	18
Details	BINDING: BINDING => ECO:0000269\|PubMed:12505993, ECO:0000269\|PubMed:15939019, ECO:0007744\|PDB:1MX0, ECO:0007744\|PDB:1Z59, ECO:0007744\|PDB:1Z5A, ECO:0007744\|PDB:1Z5B, ECO:0007744\|PDB:1Z5C

Chain	Residue	Details
A	ASN42
D	ASN42
D	ASP76
D	MSE107
E	ASN42
E	ASP76
E	MSE107
F	ASN42
F	ASP76
F	MSE107
A	ASP76
A	MSE107
B	ASN42
B	ASP76
B	MSE107
C	ASN42
C	ASP76
C	MSE107

site_id	SWS_FT_FI2
Number of Residues	6
Details	BINDING: BINDING => ECO:0000269\|PubMed:12505993, ECO:0000269\|PubMed:15939019, ECO:0007744\|PDB:1MX0, ECO:0007744\|PDB:1Z5A, ECO:0007744\|PDB:1Z5B, ECO:0007744\|PDB:1Z5C

Chain	Residue	Details
A	SER96
B	SER96
C	SER96
D	SER96
E	SER96
F	SER96

site_id	SWS_FT_FI3
Number of Residues	6
Details	BINDING: BINDING => ECO:0000269\|PubMed:12505993, ECO:0007744\|PDB:1MX0

Chain	Residue	Details
A	LYS427
B	LYS427
C	LYS427
D	LYS427
E	LYS427
F	LYS427

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)