Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

3ZKB

CRYSTAL STRUCTURE OF THE ATPASE REGION OF Mycobacterium tuberculosis GyrB WITH AMPPNP

Functional Information from GO Data

Chain	GOid	namespace	contents
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	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	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	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	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	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
G	0003677	molecular_function	DNA binding
G	0003918	molecular_function	DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) activity
G	0005524	molecular_function	ATP binding
G	0006265	biological_process	DNA topological change
H	0003677	molecular_function	DNA binding
H	0003918	molecular_function	DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) activity
H	0005524	molecular_function	ATP binding
H	0006265	biological_process	DNA topological change
I	0003677	molecular_function	DNA binding
I	0003918	molecular_function	DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) activity
I	0005524	molecular_function	ATP binding
I	0006265	biological_process	DNA topological change
J	0003677	molecular_function	DNA binding
J	0003918	molecular_function	DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) activity
J	0005524	molecular_function	ATP binding
J	0006265	biological_process	DNA topological change
K	0003677	molecular_function	DNA binding
K	0003918	molecular_function	DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) activity
K	0005524	molecular_function	ATP binding
K	0006265	biological_process	DNA topological change
L	0003677	molecular_function	DNA binding
L	0003918	molecular_function	DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) activity
L	0005524	molecular_function	ATP binding
L	0006265	biological_process	DNA topological change
M	0003677	molecular_function	DNA binding
M	0003918	molecular_function	DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) activity
M	0005524	molecular_function	ATP binding
M	0006265	biological_process	DNA topological change
N	0003677	molecular_function	DNA binding
N	0003918	molecular_function	DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) activity
N	0005524	molecular_function	ATP binding
N	0006265	biological_process	DNA topological change
O	0003677	molecular_function	DNA binding
O	0003918	molecular_function	DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) activity
O	0005524	molecular_function	ATP binding
O	0006265	biological_process	DNA topological change
P	0003677	molecular_function	DNA binding
P	0003918	molecular_function	DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) activity
P	0005524	molecular_function	ATP binding
P	0006265	biological_process	DNA topological change

Functional Information from PDB Data

site_id	AC1
Number of Residues	31
Details	BINDING SITE FOR RESIDUE ANP A 601

Chain	Residue
A	GLU48
A	GLY107
A	LYS108
A	TYR114
A	GLY119
A	LEU120
A	HIS121
A	GLY122
A	VAL123
A	GLY124
A	VAL125
A	ASN52
A	SER169
A	GLN370
A	LYS372
A	MG602
A	HOH2010
A	HOH2012
A	HOH2013
A	HOH2016
A	HOH2019
A	HOH2021
A	GLU56
B	TYR12
B	ILE17
A	ASP79
A	GLY83
A	ILE84
A	VAL99
A	ALA105
A	GLY106

site_id	AC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG A 602

Chain	Residue
A	ASN52
A	LYS108
A	GLY119
A	ANP601
A	HOH2010

site_id	AC3
Number of Residues	26
Details	BINDING SITE FOR RESIDUE ANP B 601

Chain	Residue
A	TYR12
A	ILE17
B	GLU48
B	ASN52
B	GLU56
B	ASP79
B	ILE84
B	VAL99
B	ALA105
B	GLY106
B	GLY107
B	LYS108
B	TYR114
B	GLY119
B	LEU120
B	HIS121
B	GLY122
B	VAL123
B	GLY124
B	VAL125
B	GLN370
B	LYS372
B	MG602
B	HOH2002
B	HOH2006
B	HOH2009

site_id	AC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MG B 602

Chain	Residue
B	GLU48
B	ASN52
B	ANP601
B	HOH2002

site_id	AC5
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MG B 1001

Chain	Residue
B	TYR61
B	ASP80
B	GLY81
B	THR167

site_id	AC6
Number of Residues	29
Details	BINDING SITE FOR RESIDUE ANP C 601

Chain	Residue
C	ASN52
C	GLU56
C	ASP79
C	ILE84
C	VAL99
C	GLY106
C	GLY107
C	LYS108
C	TYR114
C	GLY119
C	LEU120
C	HIS121
C	GLY122
C	VAL123
C	GLY124
C	VAL125
C	SER169
C	GLN370
C	LYS372
C	MG602
C	HOH2012
C	HOH2013
C	HOH2014
C	HOH2017
C	HOH2018
C	HOH2027
C	HOH2030
D	TYR12
D	ILE17

site_id	AC7
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MG C 602

Chain	Residue
C	ASN52
C	ANP601
C	HOH2012
C	HOH2017

site_id	AC8
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG C 1001

Chain	Residue
C	ASP110
C	SER111
C	TYR114
C	SER117
C	HOH2032
C	HOH2033

site_id	AC9
Number of Residues	26
Details	BINDING SITE FOR RESIDUE ANP D 601

Chain	Residue
C	TYR12
C	ILE17
D	GLU48
D	ASN52
D	GLU56
D	ASP79
D	ILE84
D	VAL99
D	GLY106
D	GLY107
D	LYS108
D	TYR114
D	GLY119
D	LEU120
D	HIS121
D	GLY122
D	VAL123
D	GLY124
D	VAL125
D	GLN370
D	LYS372
D	MG602
D	HOH2008
D	HOH2014
D	HOH2015
D	HOH2016

site_id	BC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MG D 602

Chain	Residue
D	GLU48
D	ASN52
D	ANP601
D	HOH2008

site_id	BC2
Number of Residues	3
Details	BINDING SITE FOR RESIDUE MG D 1001

Chain	Residue
D	ASP80
D	GLY81
D	THR167

site_id	BC3
Number of Residues	30
Details	BINDING SITE FOR RESIDUE ANP E 601

Chain	Residue
E	GLU48
E	ASN52
E	GLU56
E	ASP79
E	GLY83
E	ILE84
E	VAL99
E	ALA105
E	GLY106
E	GLY107
E	LYS108
E	TYR114
E	GLY119
E	LEU120
E	HIS121
E	GLY122
E	VAL123
E	GLY124
E	VAL125
E	SER126
E	SER169
E	GLN370
E	LYS372
E	MG602
E	HOH2010
E	HOH2014
E	HOH2020
E	HOH2023
F	TYR12
F	ILE17

site_id	BC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MG E 602

Chain	Residue
E	ASN52
E	ANP601
E	HOH2010
E	HOH2014

site_id	BC5
Number of Residues	29
Details	BINDING SITE FOR RESIDUE ANP F 601

Chain	Residue
E	TYR12
E	ILE17
F	GLU48
F	ASN52
F	GLU56
F	ASP79
F	GLY83
F	ILE84
F	VAL99
F	ALA105
F	GLY106
F	GLY107
F	LYS108
F	TYR114
F	GLY119
F	LEU120
F	HIS121
F	GLY122
F	VAL123
F	GLY124
F	VAL125
F	SER169
F	GLN370
F	LYS372
F	MG602
F	HOH2003
F	HOH2005
F	HOH2008
F	HOH2009

site_id	BC6
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MG F 602

Chain	Residue
F	GLU48
F	ASN52
F	ANP601
F	HOH2003

site_id	BC7
Number of Residues	28
Details	BINDING SITE FOR RESIDUE ANP G 601

Chain	Residue
G	ASN52
G	GLU56
G	ASP79
G	ILE84
G	VAL99
G	ALA105
G	GLY106
G	GLY107
G	LYS108
G	TYR114
G	GLY119
G	LEU120
G	HIS121
G	GLY122
G	VAL123
G	GLY124
G	VAL125
G	SER126
G	SER169
G	GLN370
G	LYS372
G	MG602
G	HOH2006
G	HOH2008
G	HOH2012
G	HOH2014
H	TYR12
H	ILE17

site_id	BC8
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MG G 602

Chain	Residue
G	ASN52
G	ANP601
G	HOH2006
G	HOH2009

site_id	BC9
Number of Residues	3
Details	BINDING SITE FOR RESIDUE MG G 1001

Chain	Residue
G	ASP80
G	GLY81
G	THR167

site_id	CC1
Number of Residues	29
Details	BINDING SITE FOR RESIDUE ANP H 601

Chain	Residue
G	TYR12
G	ILE17
H	GLU48
H	ASN52
H	GLU56
H	ASP79
H	ILE84
H	VAL99
H	ALA105
H	GLY106
H	GLY107
H	LYS108
H	TYR114
H	GLY119
H	LEU120
H	HIS121
H	GLY122
H	VAL123
H	GLY124
H	VAL125
H	SER169
H	GLN370
H	LYS372
H	MG602
H	HOH2002
H	HOH2003
H	HOH2006
H	HOH2007
H	HOH2008

site_id	CC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MG H 602

Chain	Residue
H	ASN52
H	GLY119
H	ANP601
H	HOH2002

site_id	CC3
Number of Residues	27
Details	BINDING SITE FOR RESIDUE ANP I 601

Chain	Residue
I	GLU48
I	ASN52
I	GLU56
I	ASP79
I	ILE84
I	VAL99
I	ALA105
I	GLY106
I	GLY107
I	LYS108
I	TYR114
I	GLY119
I	LEU120
I	HIS121
I	GLY122
I	VAL123
I	GLY124
I	VAL125
I	SER169
I	GLN370
I	LYS372
I	MG602
I	HOH2006
I	HOH2012
I	HOH2015
J	TYR12
J	ILE17

site_id	CC4
Number of Residues	3
Details	BINDING SITE FOR RESIDUE MG I 602

Chain	Residue
I	GLU48
I	ASN52
I	ANP601

site_id	CC5
Number of Residues	27
Details	BINDING SITE FOR RESIDUE ANP J 601

Chain	Residue
I	TYR12
I	ILE17
J	GLU48
J	ASN52
J	GLU56
J	ASP79
J	ILE84
J	VAL99
J	ALA105
J	GLY106
J	GLY107
J	LYS108
J	TYR114
J	GLY119
J	LEU120
J	HIS121
J	GLY122
J	VAL123
J	GLY124
J	VAL125
J	GLN370
J	LYS372
J	MG602
J	HOH2010
J	HOH2011
J	HOH2014
J	HOH2015

site_id	CC6
Number of Residues	3
Details	BINDING SITE FOR RESIDUE MG J 602

Chain	Residue
J	GLU48
J	ASN52
J	ANP601

site_id	CC7
Number of Residues	28
Details	BINDING SITE FOR RESIDUE ANP K 601

Chain	Residue
K	GLU48
K	ASN52
K	GLU56
K	ASP79
K	ILE84
K	VAL99
K	ALA105
K	GLY106
K	GLY107
K	LYS108
K	TYR114
K	GLY119
K	LEU120
K	HIS121
K	GLY122
K	VAL123
K	GLY124
K	VAL125
K	SER126
K	SER169
K	GLN370
K	LYS372
K	MG602
K	HOH2004
K	HOH2006
K	HOH2007
L	TYR12
L	ILE17

site_id	CC8
Number of Residues	3
Details	BINDING SITE FOR RESIDUE MG K 602

Chain	Residue
K	GLU48
K	ASN52
K	ANP601

site_id	CC9
Number of Residues	27
Details	BINDING SITE FOR RESIDUE ANP L 601

Chain	Residue
K	TYR12
K	ILE17
L	GLU48
L	ASN52
L	GLU56
L	ASP79
L	ILE84
L	VAL99
L	ALA105
L	GLY106
L	GLY107
L	LYS108
L	TYR114
L	GLY119
L	LEU120
L	HIS121
L	GLY122
L	VAL123
L	GLY124
L	VAL125
L	SER169
L	GLN370
L	LYS372
L	MG602
L	HOH2005
L	HOH2007
L	HOH2008

site_id	DC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG L 602

Chain	Residue
L	GLU48
L	ASN52
L	ANP601
L	HOH2003
L	HOH2005

site_id	DC2
Number of Residues	27
Details	BINDING SITE FOR RESIDUE ANP M 601

Chain	Residue
M	GLU48
M	ASN52
M	ASP79
M	GLY83
M	ILE84
M	VAL99
M	ALA105
M	GLY106
M	GLY107
M	LYS108
M	TYR114
M	GLY119
M	LEU120
M	HIS121
M	GLY122
M	VAL123
M	GLY124
M	VAL125
M	SER126
M	GLN370
M	LYS372
M	MG602
M	HOH2002
M	HOH2004
M	HOH2005
N	TYR12
N	ILE17

site_id	DC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MG M 602

Chain	Residue
M	GLU48
M	ASN52
M	ANP601
M	HOH2002

site_id	DC4
Number of Residues	27
Details	BINDING SITE FOR RESIDUE ANP N 601

Chain	Residue
M	TYR12
M	ILE17
N	GLU48
N	ASN52
N	GLU56
N	ASP79
N	GLY83
N	ILE84
N	VAL99
N	ALA105
N	GLY106
N	GLY107
N	LYS108
N	TYR114
N	GLY119
N	LEU120
N	HIS121
N	GLY122
N	VAL123
N	GLY124
N	VAL125
N	SER169
N	GLN370
N	LYS372
N	MG602
N	HOH2003
N	HOH2007

site_id	DC5
Number of Residues	3
Details	BINDING SITE FOR RESIDUE MG N 602

Chain	Residue
N	ASN52
N	ANP601
N	HOH2003

site_id	DC6
Number of Residues	25
Details	BINDING SITE FOR RESIDUE ANP O 601

Chain	Residue
O	GLU48
O	ASN52
O	GLU56
O	ASP79
O	GLY83
O	ILE84
O	VAL99
O	GLY106
O	GLY107
O	LYS108
O	TYR114
O	GLY119
O	LEU120
O	HIS121
O	GLY122
O	VAL123
O	GLY124
O	VAL125
O	SER126
O	SER169
O	GLN370
O	LYS372
O	MG602
P	TYR12
P	ILE17

site_id	DC7
Number of Residues	3
Details	BINDING SITE FOR RESIDUE MG O 602

Chain	Residue
O	GLU48
O	ASN52
O	ANP601

site_id	DC8
Number of Residues	24
Details	BINDING SITE FOR RESIDUE ANP P 601

Chain	Residue
O	TYR12
P	GLU48
P	ASN52
P	GLU56
P	ASP79
P	GLY83
P	ILE84
P	VAL99
P	GLY107
P	LYS108
P	TYR114
P	GLY119
P	LEU120
P	HIS121
P	GLY122
P	VAL123
P	GLY124
P	VAL125
P	SER169
P	GLN370
P	LYS372
P	MG602
P	HOH2002
P	HOH2004

site_id	DC9
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MG P 602

Chain	Residue
P	GLU48
P	ASN52
P	ANP601
P	HOH2001

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	224
Details	Binding site: {"evidences":[{"source":"PubMed","id":"24015710","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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