3ZM7

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

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

Functional Information from PDB Data

site_id	AC1
Number of Residues	13
Details	BINDING SITE FOR RESIDUE ACP A 525

Chain	Residue
A	GLU48
A	SER169
A	MG526
A	HOH2004
A	HOH2005
A	ASN52
A	GLU56
A	ASP79
A	GLY83
A	ILE84
A	VAL99
A	GLY124
A	VAL125

---

site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MG A 526

Chain	Residue
A	GLU48
A	ASN52
A	ACP525
A	HOH2004

---

site_id	AC3
Number of Residues	11
Details	BINDING SITE FOR RESIDUE ACP B 525

Chain	Residue
B	ASN52
B	GLU56
B	ILE84
B	VAL99
B	VAL123
B	GLY124
B	VAL125
B	SER169
B	MG526
B	HOH2002
B	HOH2003

---

site_id	AC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MG B 526

Chain	Residue
B	ASN52
B	ACP525
B	HOH2002
B	HOH2003

---

site_id	AC5
Number of Residues	13
Details	BINDING SITE FOR RESIDUE ACP C 525

Chain	Residue
C	GLU48
C	ASN52
C	GLU56
C	ASP79
C	GLY83
C	ILE84
C	VAL123
C	GLY124
C	VAL125
C	SER169
C	MG526
C	HOH2001
C	HOH2002

---

site_id	AC6
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG C 526

Chain	Residue
C	GLU48
C	ASN52
C	ACP525
C	HOH2001
C	HOH2002

---

site_id	AC7
Number of Residues	13
Details	BINDING SITE FOR RESIDUE ACP D 525

Chain	Residue
D	GLU48
D	ASN52
D	GLU56
D	ASP79
D	GLY83
D	ILE84
D	VAL99
D	GLY122
D	GLY124
D	VAL125
D	SER169
D	MG526
D	HOH2001

---

site_id	AC8
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MG D 526

Chain	Residue
D	ASN52
D	ACP525
D	HOH2001
D	HOH2002

---

site_id	AC9
Number of Residues	12
Details	BINDING SITE FOR RESIDUE ACP E 525

Chain	Residue
E	GLU48
E	ASN52
E	GLU56
E	GLY83
E	ILE84
E	VAL99
E	GLY124
E	VAL125
E	SER169
E	MG526
E	HOH2003
E	HOH2004

---

site_id	BC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MG E 526

Chain	Residue
E	ASN52
E	ACP525
E	HOH2003
E	HOH2004

---

site_id	BC2
Number of Residues	11
Details	BINDING SITE FOR RESIDUE ACP F 525

Chain	Residue
F	GLU48
F	ASN52
F	GLU56
F	ASP79
F	ILE84
F	VAL99
F	VAL123
F	GLY124
F	VAL125
F	SER169
F	MG526

---

site_id	BC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG F 526

Chain	Residue
F	GLU48
F	ASN52
F	GLY124
F	VAL125
F	ACP525

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	54
Details	BINDING: BINDING => ECO:0000269|PubMed:24015710

Chain	Residue	Details
A	TYR12
B	TYR12
B	ASN52
B	ASP79
B	GLY83
B	GLY107
B	TYR114
B	LEU120
B	SER169
B	GLN370
C	TYR12
A	ASN52
C	ASN52
C	ASP79
C	GLY83
C	GLY107
C	TYR114
C	LEU120
C	SER169
C	GLN370
D	TYR12
D	ASN52
A	ASP79
D	ASP79
D	GLY83
D	GLY107
D	TYR114
D	LEU120
D	SER169
D	GLN370
E	TYR12
E	ASN52
E	ASP79
A	GLY83
E	GLY83
E	GLY107
E	TYR114
E	LEU120
E	SER169
E	GLN370
F	TYR12
F	ASN52
F	ASP79
F	GLY83
A	GLY107
F	GLY107
F	TYR114
F	LEU120
F	SER169
F	GLN370
A	TYR114
A	LEU120
A	SER169
A	GLN370

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