3ZKD

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

Functional Information from PDB Data

site_id	AC1
Number of Residues	30
Details	BINDING SITE FOR RESIDUE ANP A 601

Chain	Residue
A	ASN52
A	TYR114
A	GLY119
A	LEU120
A	HIS121
A	GLY122
A	VAL123
A	GLY124
A	VAL125
A	SER126
A	SER169
A	GLU56
A	GLN370
A	LYS372
A	MG602
A	HOH2004
A	HOH2006
A	HOH2008
A	HOH2010
A	HOH2011
A	HOH2012
B	TYR12
A	ASP79
B	ILE17
A	GLY83
A	ILE84
A	VAL99
A	GLY106
A	GLY107
A	LYS108

---

site_id	AC2
Number of Residues	3
Details	BINDING SITE FOR RESIDUE MG A 602

Chain	Residue
A	ASN52
A	ANP601
A	HOH2006

---

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	SER169
B	GLN370
B	LYS372
B	MG602
B	HOH2005
B	HOH2007

---

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

Chain	Residue
B	GLU48
B	ASN52
B	ANP601
B	HOH2005

---

site_id	AC5
Number of Residues	30
Details	BINDING SITE FOR RESIDUE ANP C 601

Chain	Residue
C	GLU48
C	ASN52
C	GLU56
C	ASP79
C	GLY83
C	ILE84
C	VAL99
C	ALA105
C	GLY106
C	GLY107
C	LYS108
C	TYR114
C	GLY119
C	LEU120
C	HIS121
C	GLY122
C	VAL123
C	GLY124
C	VAL125
C	SER126
C	SER169
C	GLN370
C	LYS372
C	MG602
C	HOH2004
C	HOH2011
C	HOH2012
C	HOH2013
D	TYR12
D	ILE17

---

site_id	AC6
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG C 602

Chain	Residue
C	ASN52
C	GLY119
C	ANP601
C	HOH2004
C	HOH2008

---

site_id	AC7
Number of Residues	26
Details	BINDING SITE FOR RESIDUE ANP D 601

Chain	Residue
D	GLU48
D	ASN52
D	GLU56
D	ASP79
D	GLY83
D	ILE84
D	VAL99
D	ALA105
D	GLY106
D	GLY107
D	LYS108
D	TYR114
D	GLY119
D	LEU120
D	HIS121
D	GLY122
D	VAL123
D	GLY124
D	VAL125
D	SER126
D	SER169
D	GLN370
D	LYS372
D	MG602
D	HOH2002
C	TYR12

---

site_id	AC8
Number of Residues	2
Details	BINDING SITE FOR RESIDUE MG D 602

Chain	Residue
D	ASN52
D	ANP601

---

site_id	AC9
Number of Residues	28
Details	BINDING SITE FOR RESIDUE ANP E 601

Chain	Residue
E	GLU48
E	ASN52
E	GLU56
E	ASP79
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	SER169
E	GLN370
E	LYS372
E	MG602
E	HOH2006
E	HOH2007
E	HOH2009
E	HOH2012
F	TYR12
F	ILE17

---

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

Chain	Residue
E	GLU48
E	ASN52
E	ANP601
E	HOH2006

---

site_id	BC2
Number of Residues	30
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	SER126
F	SER169
F	GLN370
F	LYS372
F	MG602
F	HOH2004
F	HOH2005
F	HOH2007
F	HOH2009

---

site_id	BC3
Number of Residues	3
Details	BINDING SITE FOR RESIDUE MG F 602

Chain	Residue
F	GLU48
F	ASN52
F	ANP601

---

site_id	BC4
Number of Residues	30
Details	BINDING SITE FOR RESIDUE ANP G 601

Chain	Residue
G	GLU48
G	ASN52
G	GLU56
G	ASP79
G	GLY83
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	GLN370
G	LYS372
G	MG602
G	HOH2002
G	HOH2003
G	HOH2005
G	HOH2010
G	HOH2011
G	HOH2012
H	TYR12
H	ILE17

---

site_id	BC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG G 602

Chain	Residue
G	GLU48
G	ASN52
G	GLY124
G	ANP601
G	HOH2005

---

site_id	BC6
Number of Residues	25
Details	BINDING SITE FOR RESIDUE ANP H 601

Chain	Residue
G	TYR12
G	ILE17
H	GLU48
H	ASN52
H	GLU56
H	ASP79
H	GLY83
H	ILE84
H	VAL99
H	ALA105
H	GLY107
H	LYS108
H	TYR114
H	GLY119
H	LEU120
H	HIS121
H	GLY122
H	VAL123
H	GLY124
H	VAL125
H	SER126
H	SER169
H	GLN370
H	LYS372
H	MG602

---

site_id	BC7
Number of Residues	3
Details	BINDING SITE FOR RESIDUE MG H 602

Chain	Residue
H	GLU48
H	ASN52
H	ANP601

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	112
Details	Binding site: {"evidences":[{"source":"PubMed","id":"24015710","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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