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7DSX

Structure of a human NHE1-CHP1 complex under pH 7.5, bound by cariporide

Functional Information from GO Data
ChainGOidnamespacecontents
A0006812biological_processmonoatomic cation transport
A0006814biological_processsodium ion transport
A0006885biological_processregulation of pH
A0015297molecular_functionantiporter activity
A0015385molecular_functionsodium:proton antiporter activity
A0016020cellular_componentmembrane
A0055085biological_processtransmembrane transport
A1902600biological_processproton transmembrane transport
B0006812biological_processmonoatomic cation transport
B0006814biological_processsodium ion transport
B0006885biological_processregulation of pH
B0015297molecular_functionantiporter activity
B0015385molecular_functionsodium:proton antiporter activity
B0016020cellular_componentmembrane
B0055085biological_processtransmembrane transport
B1902600biological_processproton transmembrane transport
C0000139cellular_componentGolgi membrane
C0001578biological_processmicrotubule bundle formation
C0001933biological_processnegative regulation of protein phosphorylation
C0004860molecular_functionprotein kinase inhibitor activity
C0005509molecular_functioncalcium ion binding
C0005515molecular_functionprotein binding
C0005634cellular_componentnucleus
C0005737cellular_componentcytoplasm
C0005783cellular_componentendoplasmic reticulum
C0005793cellular_componentendoplasmic reticulum-Golgi intermediate compartment
C0005856cellular_componentcytoskeleton
C0005886cellular_componentplasma membrane
C0005925cellular_componentfocal adhesion
C0006469biological_processnegative regulation of protein kinase activity
C0006611biological_processprotein export from nucleus
C0006813biological_processpotassium ion transport
C0007264biological_processsmall GTPase-mediated signal transduction
C0008017molecular_functionmicrotubule binding
C0010923biological_processnegative regulation of phosphatase activity
C0012505cellular_componentendomembrane system
C0015031biological_processprotein transport
C0015385molecular_functionsodium:proton antiporter activity
C0015459molecular_functionpotassium channel regulator activity
C0015630cellular_componentmicrotubule cytoskeleton
C0019900molecular_functionkinase binding
C0022406biological_processmembrane docking
C0030133cellular_componenttransport vesicle
C0031122biological_processcytoplasmic microtubule organization
C0031397biological_processnegative regulation of protein ubiquitination
C0031953biological_processnegative regulation of protein autophosphorylation
C0032088biological_processnegative regulation of NF-kappaB transcription factor activity
C0032417biological_processpositive regulation of sodium:proton antiporter activity
C0035725biological_processsodium ion transmembrane transport
C0042308biological_processnegative regulation of protein import into nucleus
C0045121cellular_componentmembrane raft
C0046872molecular_functionmetal ion binding
C0048306molecular_functioncalcium-dependent protein binding
C0050821biological_processprotein stabilization
C0051222biological_processpositive regulation of protein transport
C0051453biological_processregulation of intracellular pH
C0060050biological_processpositive regulation of protein glycosylation
C0061024biological_processmembrane organization
C0061025biological_processmembrane fusion
C0070062cellular_componentextracellular exosome
C0070885biological_processnegative regulation of calcineurin-NFAT signaling cascade
C0071073biological_processpositive regulation of phospholipid biosynthetic process
C0071468biological_processcellular response to acidic pH
C0090314biological_processpositive regulation of protein targeting to membrane
C1990351cellular_componenttransporter complex
D0000139cellular_componentGolgi membrane
D0001578biological_processmicrotubule bundle formation
D0001933biological_processnegative regulation of protein phosphorylation
D0004860molecular_functionprotein kinase inhibitor activity
D0005509molecular_functioncalcium ion binding
D0005515molecular_functionprotein binding
D0005634cellular_componentnucleus
D0005737cellular_componentcytoplasm
D0005783cellular_componentendoplasmic reticulum
D0005793cellular_componentendoplasmic reticulum-Golgi intermediate compartment
D0005856cellular_componentcytoskeleton
D0005886cellular_componentplasma membrane
D0005925cellular_componentfocal adhesion
D0006469biological_processnegative regulation of protein kinase activity
D0006611biological_processprotein export from nucleus
D0006813biological_processpotassium ion transport
D0007264biological_processsmall GTPase-mediated signal transduction
D0008017molecular_functionmicrotubule binding
D0010923biological_processnegative regulation of phosphatase activity
D0012505cellular_componentendomembrane system
D0015031biological_processprotein transport
D0015385molecular_functionsodium:proton antiporter activity
D0015459molecular_functionpotassium channel regulator activity
D0015630cellular_componentmicrotubule cytoskeleton
D0019900molecular_functionkinase binding
D0022406biological_processmembrane docking
D0030133cellular_componenttransport vesicle
D0031122biological_processcytoplasmic microtubule organization
D0031397biological_processnegative regulation of protein ubiquitination
D0031953biological_processnegative regulation of protein autophosphorylation
D0032088biological_processnegative regulation of NF-kappaB transcription factor activity
D0032417biological_processpositive regulation of sodium:proton antiporter activity
D0035725biological_processsodium ion transmembrane transport
D0042308biological_processnegative regulation of protein import into nucleus
D0045121cellular_componentmembrane raft
D0046872molecular_functionmetal ion binding
D0048306molecular_functioncalcium-dependent protein binding
D0050821biological_processprotein stabilization
D0051222biological_processpositive regulation of protein transport
D0051453biological_processregulation of intracellular pH
D0060050biological_processpositive regulation of protein glycosylation
D0061024biological_processmembrane organization
D0061025biological_processmembrane fusion
D0070062cellular_componentextracellular exosome
D0070885biological_processnegative regulation of calcineurin-NFAT signaling cascade
D0071073biological_processpositive regulation of phospholipid biosynthetic process
D0071468biological_processcellular response to acidic pH
D0090314biological_processpositive regulation of protein targeting to membrane
D1990351cellular_componenttransporter complex
Functional Information from PDB Data
site_idAC1
Number of Residues10
Detailsbinding site for residue PGT B 1001
ChainResidue
ALEU332
BPGT1002
APGT601
BTRP108
BILE109
BMET385
BTRP386
BVAL389
BLEU393
BPHE397

site_idAC2
Number of Residues7
Detailsbinding site for residue PGT B 1002
ChainResidue
BILE105
BVAL160
BPHE164
BTYR339
BTRP386
BPGT1001
BPGT1004

site_idAC3
Number of Residues9
Detailsbinding site for residue HG0 B 1003
ChainResidue
AASP95
BSER158
BASP159
BPHE162
BLEU163
BASP267
BVAL271
BGLU346
BLEU468

site_idAC4
Number of Residues6
Detailsbinding site for residue PGT B 1004
ChainResidue
AILE105
APGT601
APGT602
BPHE335
BTYR339
BPGT1002

site_idAC5
Number of Residues6
Detailsbinding site for residue PGT A 601
ChainResidue
APHE335
ATYR339
APGT603
BILE105
BPGT1001
BPGT1004

site_idAC6
Number of Residues10
Detailsbinding site for residue PGT A 602
ChainResidue
ATRP108
AILE109
AMET385
ATRP386
AVAL389
ALEU393
APHE397
APGT603
BLEU332
BPGT1004

site_idAC7
Number of Residues7
Detailsbinding site for residue PGT A 603
ChainResidue
AILE105
AVAL160
APHE164
ATYR339
ATRP386
APGT601
APGT602

site_idAC8
Number of Residues9
Detailsbinding site for residue HG0 A 604
ChainResidue
ASER158
AASP159
APHE162
ALEU163
AASP267
AVAL271
AGLU346
ALEU468
BASP95

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues44
DetailsTRANSMEM: Helical; Name=1 => ECO:0000269|PubMed:34108458, ECO:0007744|PDB:7DSW
ChainResidueDetails
BVAL99-VAL121
CASP123
CASP125
CASP127
CLYS129
CGLU134
CASP164
CASP166
CASP168
CGLU175
AVAL99-VAL121
DASP127
DLYS129
DGLU134
DASP164
DASP166
DASP168
DGLU175

site_idSWS_FT_FI2
Number of Residues60
DetailsTOPO_DOM: Cytoplasmic => ECO:0000305
ChainResidueDetails
BILE122-PRO130
ATHR323-VAL328
ASER372-HIS373
APHE439-LEU444
BLEU177-LEU186
BHIS250-ASN252
BTHR323-VAL328
BSER372-HIS373
BPHE439-LEU444
AILE122-PRO130
ALEU177-LEU186
AHIS250-ASN252

site_idSWS_FT_FI3
Number of Residues34
DetailsTRANSMEM: Helical; Name=2 => ECO:0000269|PubMed:34108458, ECO:0007744|PDB:7DSW
ChainResidueDetails
BGLU131-GLY148
AGLU131-GLY148

site_idSWS_FT_FI4
Number of Residues72
DetailsTOPO_DOM: Extracellular => ECO:0000305
ChainResidueDetails
BVAL149-SER158
ATYR342-LEU350
AGLY405-ASN410
AASP470-PRO475
BGLY216-ILE222
BGLU284-GLY287
BTYR342-LEU350
BGLY405-ASN410
BASP470-PRO475
AVAL149-SER158
AGLY216-ILE222
AGLU284-GLY287

site_idSWS_FT_FI5
Number of Residues34
DetailsTRANSMEM: Helical; Name=3 => ECO:0000269|PubMed:34108458, ECO:0007744|PDB:7DSW
ChainResidueDetails
BASP159-PHE176
AASP159-PHE176

site_idSWS_FT_FI6
Number of Residues56
DetailsTRANSMEM: Helical; Name=4 => ECO:0000269|PubMed:34108458, ECO:0007744|PDB:7DSW
ChainResidueDetails
BGLY187-GLY215
AGLY187-GLY215

site_idSWS_FT_FI7
Number of Residues52
DetailsTRANSMEM: Helical; Name=5 => ECO:0000269|PubMed:34108458, ECO:0007744|PDB:7DSW
ChainResidueDetails
BGLY223-ILE249
AGLY223-ILE249

site_idSWS_FT_FI8
Number of Residues60
DetailsTRANSMEM: Helical; Name=6 => ECO:0000269|PubMed:34108458, ECO:0007744|PDB:7DSW
ChainResidueDetails
BGLU253-TYR283
AGLU253-TYR283

site_idSWS_FT_FI9
Number of Residues68
DetailsTRANSMEM: Helical; Name=7 => ECO:0000269|PubMed:34108458, ECO:0007744|PDB:7DSW
ChainResidueDetails
BILE288-PHE322
AILE288-PHE322

site_idSWS_FT_FI10
Number of Residues24
DetailsTRANSMEM: Helical; Name=8 => ECO:0000269|PubMed:34108458, ECO:0007744|PDB:7DSW
ChainResidueDetails
BILE329-ALA341
AILE329-ALA341

site_idSWS_FT_FI11
Number of Residues40
DetailsTRANSMEM: Helical; Name=9 => ECO:0000269|PubMed:34108458, ECO:0007744|PDB:7DSW
ChainResidueDetails
BSER351-ILE371
ASER351-ILE371

site_idSWS_FT_FI12
Number of Residues60
DetailsTRANSMEM: Helical; Name=10 => ECO:0000269|PubMed:34108458, ECO:0007744|PDB:7DSW
ChainResidueDetails
BLYS374-ALA404
ALYS374-ALA404

site_idSWS_FT_FI13
Number of Residues54
DetailsTRANSMEM: Helical; Name=11 => ECO:0000269|PubMed:34108458, ECO:0007744|PDB:7DSW
ChainResidueDetails
BTRP411-LYS438
ATRP411-LYS438

site_idSWS_FT_FI14
Number of Residues48
DetailsTRANSMEM: Helical; Name=12 => ECO:0000269|PubMed:34108458, ECO:0007744|PDB:7DSW
ChainResidueDetails
BTHR445-LEU469
ATHR445-LEU469

site_idSWS_FT_FI15
Number of Residues58
DetailsTRANSMEM: Helical; Name=13 => ECO:0000269|PubMed:34108458, ECO:0007744|PDB:7DSW
ChainResidueDetails
BMET476-LEU505
AMET476-LEU505

site_idSWS_FT_FI16
Number of Residues2
DetailsSITE: Channel pore-lining => ECO:0000305
ChainResidueDetails
BPHE161
APHE161

site_idSWS_FT_FI17
Number of Residues2
DetailsSITE: Not glycosylated
ChainResidueDetails
BASN370
AASN370

222415

PDB entries from 2024-07-10

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