Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

4AU5

Structure of the NhaA dimer, crystallised at low pH

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005886	cellular_component	plasma membrane
A	0006814	biological_process	sodium ion transport
A	0006885	biological_process	regulation of pH
A	0009651	biological_process	response to salt stress
A	0010446	biological_process	response to alkaline pH
A	0015081	molecular_function	sodium ion transmembrane transporter activity
A	0015297	molecular_function	antiporter activity
A	0015385	molecular_function	sodium:proton antiporter activity
A	0016020	cellular_component	membrane
A	0035725	biological_process	sodium ion transmembrane transport
A	0051453	biological_process	regulation of intracellular pH
A	0055085	biological_process	transmembrane transport
A	1901612	molecular_function	cardiolipin binding
B	0005886	cellular_component	plasma membrane
B	0006814	biological_process	sodium ion transport
B	0006885	biological_process	regulation of pH
B	0009651	biological_process	response to salt stress
B	0010446	biological_process	response to alkaline pH
B	0015081	molecular_function	sodium ion transmembrane transporter activity
B	0015297	molecular_function	antiporter activity
B	0015385	molecular_function	sodium:proton antiporter activity
B	0016020	cellular_component	membrane
B	0035725	biological_process	sodium ion transmembrane transport
B	0051453	biological_process	regulation of intracellular pH
B	0055085	biological_process	transmembrane transport
B	1901612	molecular_function	cardiolipin binding
C	0005886	cellular_component	plasma membrane
C	0006814	biological_process	sodium ion transport
C	0006885	biological_process	regulation of pH
C	0009651	biological_process	response to salt stress
C	0010446	biological_process	response to alkaline pH
C	0015081	molecular_function	sodium ion transmembrane transporter activity
C	0015297	molecular_function	antiporter activity
C	0015385	molecular_function	sodium:proton antiporter activity
C	0016020	cellular_component	membrane
C	0035725	biological_process	sodium ion transmembrane transport
C	0051453	biological_process	regulation of intracellular pH
C	0055085	biological_process	transmembrane transport
C	1901612	molecular_function	cardiolipin binding
D	0005886	cellular_component	plasma membrane
D	0006814	biological_process	sodium ion transport
D	0006885	biological_process	regulation of pH
D	0009651	biological_process	response to salt stress
D	0010446	biological_process	response to alkaline pH
D	0015081	molecular_function	sodium ion transmembrane transporter activity
D	0015297	molecular_function	antiporter activity
D	0015385	molecular_function	sodium:proton antiporter activity
D	0016020	cellular_component	membrane
D	0035725	biological_process	sodium ion transmembrane transport
D	0051453	biological_process	regulation of intracellular pH
D	0055085	biological_process	transmembrane transport
D	1901612	molecular_function	cardiolipin binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE LMU B 1384

Chain	Residue
A	THR205
B	ARG250
B	TRP258
B	SO41385

site_id	AC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE SO4 B 1385

Chain	Residue
B	LMU1384
A	ARG204
A	THR205
A	GLY206
B	VAL254
B	TRP258

site_id	AC3
Number of Residues	3
Details	BINDING SITE FOR RESIDUE SO4 B 1386

Chain	Residue
B	ARG204
B	THR205
B	GLY206

site_id	AC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 C 1391

Chain	Residue
C	ARG204
C	THR205
C	GLY206
D	VAL254

site_id	AC5
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 D 1384

Chain	Residue
C	VAL254
D	ARG204
D	THR205
D	GLY206

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	380
Details	TOPO_DOM: Cytoplasmic => ECO:0000269\|PubMed:25422503, ECO:0007744\|PDB:4ATV, ECO:0007744\|PDB:4AU5

Chain	Residue	Details
A	MET1-ASP11
B	GLY201-ARG204
B	ILE237-HIS253
B	ALA311-PHE339
C	MET1-ASP11
C	ARG81-PHE96
C	ALA131-ILE154
C	GLY201-ARG204
C	ILE237-HIS253
C	ALA311-PHE339
D	MET1-ASP11
A	ARG81-PHE96
D	ARG81-PHE96
D	ALA131-ILE154
D	GLY201-ARG204
D	ILE237-HIS253
D	ALA311-PHE339
A	ALA131-ILE154
A	GLY201-ARG204
A	ILE237-HIS253
A	ALA311-PHE339
B	MET1-ASP11
B	ARG81-PHE96
B	ALA131-ILE154

site_id	SWS_FT_FI2
Number of Residues	76
Details	TRANSMEM: Helical; Name=1 => ECO:0000269\|PubMed:25422503, ECO:0007744\|PDB:4ATV, ECO:0007744\|PDB:4AU5

Chain	Residue	Details
A	ALA12-SER31
B	ALA12-SER31
C	ALA12-SER31
D	ALA12-SER31

site_id	SWS_FT_FI3
Number of Residues	216
Details	TOPO_DOM: Periplasmic => ECO:0000269\|PubMed:25422503, ECO:0007744\|PDB:4ATV, ECO:0007744\|PDB:4AU5

Chain	Residue	Details
A	GLY32-ASN58
B	GLY223
B	GLY273-SER286
B	GLY351-LEU357
C	GLY32-ASN58
C	TYR117-THR122
C	ASN177-SER180
C	GLY223
C	GLY273-SER286
C	GLY351-LEU357
D	GLY32-ASN58
A	TYR117-THR122
D	TYR117-THR122
D	ASN177-SER180
D	GLY223
D	GLY273-SER286
D	GLY351-LEU357
A	ASN177-SER180
A	GLY223
A	GLY273-SER286
A	GLY351-LEU357
B	GLY32-ASN58
B	TYR117-THR122
B	ASN177-SER180

site_id	SWS_FT_FI4
Number of Residues	84
Details	TRANSMEM: Helical; Name=2 => ECO:0000269\|PubMed:25422503, ECO:0007744\|PDB:4ATV, ECO:0007744\|PDB:4AU5

Chain	Residue	Details
A	MET59-LYS80
B	MET59-LYS80
C	MET59-LYS80
D	MET59-LYS80

site_id	SWS_FT_FI5
Number of Residues	76
Details	TRANSMEM: Helical; Name=3 => ECO:0000269\|PubMed:25422503, ECO:0007744\|PDB:4ATV, ECO:0007744\|PDB:4AU5

Chain	Residue	Details
A	PRO97-ASN116
B	PRO97-ASN116
C	PRO97-ASN116
D	PRO97-ASN116

site_id	SWS_FT_FI6
Number of Residues	28
Details	TRANSMEM: Helical; Name=4 => ECO:0000269\|PubMed:25422503, ECO:0007744\|PDB:4ATV, ECO:0007744\|PDB:4AU5

Chain	Residue	Details
A	ARG123-ALA130
B	ARG123-ALA130
C	ARG123-ALA130
D	ARG123-ALA130

site_id	SWS_FT_FI7
Number of Residues	84
Details	TRANSMEM: Helical; Name=5 => ECO:0000269\|PubMed:25422503, ECO:0007744\|PDB:4ATV, ECO:0007744\|PDB:4AU5

Chain	Residue	Details
A	PHE155-THR176
B	PHE155-THR176
C	PHE155-THR176
D	PHE155-THR176

site_id	SWS_FT_FI8
Number of Residues	76
Details	TRANSMEM: Helical; Name=6 => ECO:0000269\|PubMed:25422503, ECO:0007744\|PDB:4ATV, ECO:0007744\|PDB:4AU5

Chain	Residue	Details
A	MET181-CYS200
B	MET181-CYS200
C	MET181-CYS200
D	MET181-CYS200

site_id	SWS_FT_FI9
Number of Residues	68
Details	TRANSMEM: Helical; Name=7 => ECO:0000269\|PubMed:25422503, ECO:0007744\|PDB:4ATV, ECO:0007744\|PDB:4AU5

Chain	Residue	Details
A	THR205-SER222
B	THR205-SER222
C	THR205-SER222
D	THR205-SER222

site_id	SWS_FT_FI10
Number of Residues	48
Details	TRANSMEM: Helical; Name=8 => ECO:0000269\|PubMed:25422503, ECO:0007744\|PDB:4ATV, ECO:0007744\|PDB:4AU5

Chain	Residue	Details
A	VAL224-PHE236
B	VAL224-PHE236
C	VAL224-PHE236
D	VAL224-PHE236

site_id	SWS_FT_FI11
Number of Residues	72
Details	TRANSMEM: Helical; Name=9 => ECO:0000269\|PubMed:25422503, ECO:0007744\|PDB:4ATV, ECO:0007744\|PDB:4AU5

Chain	Residue	Details
A	VAL254-ALA272
B	VAL254-ALA272
C	VAL254-ALA272
D	VAL254-ALA272

site_id	SWS_FT_FI12
Number of Residues	92
Details	TRANSMEM: Helical; Name=10 => ECO:0000269\|PubMed:25422503, ECO:0007744\|PDB:4ATV, ECO:0007744\|PDB:4AU5

Chain	Residue	Details
A	ILE287-LEU310
B	ILE287-LEU310
C	ILE287-LEU310
D	ILE287-LEU310

site_id	SWS_FT_FI13
Number of Residues	40
Details	TRANSMEM: Helical; Name=11 => ECO:0000269\|PubMed:25422503, ECO:0007744\|PDB:4ATV, ECO:0007744\|PDB:4AU5

Chain	Residue	Details
A	THR340-PHE350
B	THR340-PHE350
C	THR340-PHE350
D	THR340-PHE350

site_id	SWS_FT_FI14
Number of Residues	88
Details	TRANSMEM: Helical; Name=12 => ECO:0000269\|PubMed:25422503, ECO:0007744\|PDB:4ATV, ECO:0007744\|PDB:4AU5

Chain	Residue	Details
A	ILE358-LEU380
B	ILE358-LEU380
C	ILE358-LEU380
D	ILE358-LEU380

site_id	SWS_FT_FI15
Number of Residues	28
Details	TOPO_DOM: Cytoplasmic => ECO:0000269\|PubMed:15919996, ECO:0000269\|PubMed:25422503, ECO:0007744\|PDB:4ATV, ECO:0007744\|PDB:4AU5

Chain	Residue	Details
A	ARG381-VAL388
B	ARG381-VAL388
C	ARG381-VAL388
D	ARG381-VAL388

site_id	SWS_FT_FI16
Number of Residues	4
Details	SITE: Important for stability, cation binding and translocation => ECO:0000305\|PubMed:15988517, ECO:0000305\|PubMed:22915592, ECO:0000305\|PubMed:27021484, ECO:0000305\|PubMed:29410365, ECO:0000305\|PubMed:7737413

Chain	Residue	Details
A	ASP133
B	ASP133
C	ASP133
D	ASP133

site_id	SWS_FT_FI17
Number of Residues	4
Details	SITE: Essential for cation binding and translocation => ECO:0000305\|PubMed:15988517, ECO:0000305\|PubMed:19274728, ECO:0000305\|PubMed:22915592, ECO:0000305\|PubMed:25422503, ECO:0000305\|PubMed:27021484, ECO:0000305\|PubMed:27708266, ECO:0000305\|PubMed:30409911, ECO:0000305\|PubMed:7737413

Chain	Residue	Details
A	ASP163
B	ASP163
C	ASP163
D	ASP163

site_id	SWS_FT_FI18
Number of Residues	4
Details	SITE: Essential for cation binding and translocation => ECO:0000305\|PubMed:15988517, ECO:0000305\|PubMed:19274728, ECO:0000305\|PubMed:22915592, ECO:0000305\|PubMed:25422503, ECO:0000305\|PubMed:27021484, ECO:0000305\|PubMed:27708266, ECO:0000305\|PubMed:7737413

Chain	Residue	Details
A	ASP164
B	ASP164
C	ASP164
D	ASP164

site_id	SWS_FT_FI19
Number of Residues	8
Details	SITE: Important for pH response => ECO:0000305\|PubMed:10455127

Chain	Residue	Details
A	GLU241
A	VAL254
B	GLU241
B	VAL254
C	GLU241
C	VAL254
D	GLU241
D	VAL254

site_id	SWS_FT_FI20
Number of Residues	4
Details	SITE: Important for pH response => ECO:0000305\|PubMed:14604993

Chain	Residue	Details
A	GLU252
B	GLU252
C	GLU252
D	GLU252

site_id	SWS_FT_FI21
Number of Residues	4
Details	SITE: Important for stability and activity => ECO:0000305\|PubMed:15988517, ECO:0000305\|PubMed:22915592, ECO:0000305\|PubMed:25422503, ECO:0000305\|PubMed:27708266, ECO:0000305\|PubMed:28330875, ECO:0000305\|PubMed:30409911

Chain	Residue	Details
A	LYS300
B	LYS300
C	LYS300
D	LYS300

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