Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

5CDQ

2.95A structure of Moxifloxacin with S.aureus DNA gyrase and DNA

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	0006259	biological_process	DNA metabolic process
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	0006259	biological_process	DNA metabolic process
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
R	0003677	molecular_function	DNA binding
R	0003918	molecular_function	DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) activity
R	0005524	molecular_function	ATP binding
R	0006259	biological_process	DNA metabolic process
R	0006265	biological_process	DNA topological change
S	0003677	molecular_function	DNA binding
S	0003918	molecular_function	DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) activity
S	0005524	molecular_function	ATP binding
S	0006265	biological_process	DNA topological change
T	0003677	molecular_function	DNA binding
T	0003918	molecular_function	DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) activity
T	0005524	molecular_function	ATP binding
T	0006259	biological_process	DNA metabolic process
T	0006265	biological_process	DNA topological change
U	0003677	molecular_function	DNA binding
U	0003918	molecular_function	DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) activity
U	0005524	molecular_function	ATP binding
U	0006265	biological_process	DNA topological change

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	binding site for residue MG A 501

Chain	Residue
E	MFX2101
E	HOH2201
E	HOH2211
E	HOH2213
F	HOH2214

site_id	AC2
Number of Residues	4
Details	binding site for residue MG A 502

Chain	Residue
A	TYR322
A	LYS323
A	THR325
A	GLN328

site_id	AC3
Number of Residues	5
Details	binding site for residue GOL A 503

Chain	Residue
A	ASP148
A	GLY152
A	ASN153
A	GLU154
A	ARG155

site_id	AC4
Number of Residues	5
Details	binding site for residue GOL A 504

Chain	Residue
A	ARG385
A	LEU388
A	ASP389
A	ARG438
A	GLU442

site_id	AC5
Number of Residues	5
Details	binding site for residue MG B 1001

Chain	Residue
B	ASP508
B	ASP510
B	HOH1107
B	HOH1111
B	HOH1116

site_id	AC6
Number of Residues	5
Details	binding site for residue MG C 501

Chain	Residue
E	HOH2214
F	MFX2101
F	HOH2201
F	HOH2208
F	HOH2213

site_id	AC7
Number of Residues	4
Details	binding site for residue MG C 502

Chain	Residue
C	TYR322
C	LYS323
C	THR325
C	GLN328

site_id	AC8
Number of Residues	5
Details	binding site for residue GOL C 503

Chain	Residue
C	ASP148
C	GLY152
C	ASN153
C	GLU154
C	ARG155

site_id	AC9
Number of Residues	4
Details	binding site for residue GOL C 504

Chain	Residue
C	ARG377
C	LEU384
C	ALA424
C	ARG432

site_id	AD1
Number of Residues	6
Details	binding site for residue MG D 1001

Chain	Residue
D	ASP508
D	ASP510
D	HOH1101
D	HOH1102
D	HOH1103
D	HOH1104

site_id	AD2
Number of Residues	13
Details	binding site for residue MFX E 2101

Chain	Residue
A	SER84
A	MG501
B	GLY459
B	GLU477
C	ARG122
E	DC2012
E	DA2013
E	HOH2201
E	HOH2211
E	HOH2213
F	DT8
F	DG2009
F	HOH2214

site_id	AD3
Number of Residues	13
Details	binding site for residue MFX F 2101

Chain	Residue
A	ARG122
A	PTR123
C	SER84
C	MG501
D	ASP437
D	ARG458
E	DT8
E	DG2009
F	DC2012
F	DA2013
F	HOH2201
F	HOH2208
F	HOH2213

site_id	AD4
Number of Residues	3
Details	binding site for residue MG F 2102

Chain	Residue
F	MFX2103
F	HOH2207
F	HOH2212

site_id	AD5
Number of Residues	6
Details	binding site for residue MFX F 2103

Chain	Residue
E	DT2019
F	DG1
F	DA2
F	MG2102
F	HOH2207
F	HOH2212

site_id	AD6
Number of Residues	5
Details	binding site for residue MG R 4301

Chain	Residue
V	MFX2101
V	HOH2201
V	HOH2204
V	HOH2206
W	HOH2210

site_id	AD7
Number of Residues	4
Details	binding site for residue GOL R 4302

Chain	Residue
R	GLY152
R	ASN153
R	GLU154
R	ARG155

site_id	AD8
Number of Residues	6
Details	binding site for residue GOL R 4303

Chain	Residue
R	ARG366
R	THR367
R	ASN370
R	TYR451
R	GLU454
R	HOH4426

site_id	AD9
Number of Residues	6
Details	binding site for residue GOL R 4304

Chain	Residue
R	ARG69
R	ASP73
T	GLN56
T	ARG69
T	ASP73
R	GLN56

site_id	AE1
Number of Residues	6
Details	binding site for residue MG S 1001

Chain	Residue
S	ASP508
S	ASP510
S	HOH1102
S	HOH1107
S	HOH1108
S	HOH1110

site_id	AE2
Number of Residues	5
Details	binding site for residue MG T 4501

Chain	Residue
V	HOH2207
W	MFX2101
W	HOH2201
W	HOH2208
W	HOH2209

site_id	AE3
Number of Residues	4
Details	binding site for residue MG T 4502

Chain	Residue
T	TYR322
T	LYS323
T	THR325
T	GLN328

site_id	AE4
Number of Residues	5
Details	binding site for residue GOL T 4503

Chain	Residue
T	ASP148
T	GLY152
T	ASN153
T	GLU154
T	ARG155

site_id	AE5
Number of Residues	6
Details	binding site for residue MG U 1001

Chain	Residue
U	ASP508
U	ASP510
U	HOH1102
U	HOH1103
U	HOH1104
U	HOH1105

site_id	AE6
Number of Residues	11
Details	binding site for residue MFX V 2101

Chain	Residue
R	SER84
R	MG4301
S	GLU477
T	ARG122
V	DC2012
V	DA2013
V	HOH2201
V	HOH2204
V	HOH2206
W	DT8
W	DG2009

site_id	AE7
Number of Residues	13
Details	binding site for residue MFX W 2101

Chain	Residue
R	ARG122
R	PTR123
T	SER84
T	MG4501
U	ASP437
U	GLU477
V	DT8
V	DG2009
W	DC2012
W	DA2013
W	HOH2201
W	HOH2208
W	HOH2209

site_id	AE8
Number of Residues	3
Details	binding site for residue MG W 2102

Chain	Residue
W	MFX2103
W	HOH2202
W	HOH2206

site_id	AE9
Number of Residues	6
Details	binding site for residue MFX W 2103

Chain	Residue
V	DT2019
W	DG1
W	DA2
W	MG2102
W	HOH2202
W	HOH2206

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
B	LEU433-GLY441

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	Active site: {"description":"O-(5'-phospho-DNA)-tyrosine intermediate","evidences":[{"source":"HAMAP-Rule","id":"MF_01897","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	456
Details	Domain: {"description":"Toprim","evidences":[{"source":"HAMAP-Rule","id":"MF_01898","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	12
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01898","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	8
Details	Site: {"description":"Interaction with DNA","evidences":[{"source":"HAMAP-Rule","id":"MF_01898","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

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