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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

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
C0006883biological_processintracellular sodium ion homeostasis
C0007264biological_processsmall GTPase-mediated signal transduction
C0008017molecular_functionmicrotubule binding
C0010560biological_processpositive regulation of glycoprotein biosynthetic process
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
C0016020cellular_componentmembrane
C0016323cellular_componentbasolateral plasma membrane
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
C0042306biological_processregulation of protein import into nucleus
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
C0061024biological_processmembrane organization
C0061025biological_processmembrane fusion
C0070062cellular_componentextracellular exosome
C0070884biological_processregulation of calcineurin-NFAT signaling cascade
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
D0006883biological_processintracellular sodium ion homeostasis
D0007264biological_processsmall GTPase-mediated signal transduction
D0008017molecular_functionmicrotubule binding
D0010560biological_processpositive regulation of glycoprotein biosynthetic process
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
D0016020cellular_componentmembrane
D0016323cellular_componentbasolateral plasma membrane
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
D0042306biological_processregulation of protein import into nucleus
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
D0061024biological_processmembrane organization
D0061025biological_processmembrane fusion
D0070062cellular_componentextracellular exosome
D0070884biological_processregulation of calcineurin-NFAT signaling cascade
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 Residues70
DetailsDomain: {"description":"EF-hand 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues70
DetailsDomain: {"description":"EF-hand 2","evidences":[{"evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues70
DetailsDomain: {"description":"EF-hand 3","evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues70
DetailsDomain: {"description":"EF-hand 4","evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues84
DetailsRegion: {"description":"Necessary for nuclear export signal"}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues18
DetailsMotif: {"description":"Nuclear export signal 1","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues18
DetailsMotif: {"description":"Nuclear export signal 2","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues18
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues44
DetailsTransmembrane: {"description":"Helical; Name=1","evidences":[{"source":"PubMed","id":"34108458","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7DSW","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues60
DetailsTopological domain: {"description":"Cytoplasmic","evidences":[{"evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI11
Number of Residues34
DetailsTransmembrane: {"description":"Helical; Name=2","evidences":[{"source":"PubMed","id":"34108458","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7DSW","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI12
Number of Residues72
DetailsTopological domain: {"description":"Extracellular","evidences":[{"evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI13
Number of Residues34
DetailsTransmembrane: {"description":"Helical; Name=3","evidences":[{"source":"PubMed","id":"34108458","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7DSW","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI14
Number of Residues56
DetailsTransmembrane: {"description":"Helical; Name=4","evidences":[{"source":"PubMed","id":"34108458","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7DSW","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI15
Number of Residues52
DetailsTransmembrane: {"description":"Helical; Name=5","evidences":[{"source":"PubMed","id":"34108458","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7DSW","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI16
Number of Residues60
DetailsTransmembrane: {"description":"Helical; Name=6","evidences":[{"source":"PubMed","id":"34108458","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7DSW","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI17
Number of Residues68
DetailsTransmembrane: {"description":"Helical; Name=7","evidences":[{"source":"PubMed","id":"34108458","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7DSW","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI18
Number of Residues24
DetailsTransmembrane: {"description":"Helical; Name=8","evidences":[{"source":"PubMed","id":"34108458","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7DSW","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI19
Number of Residues40
DetailsTransmembrane: {"description":"Helical; Name=9","evidences":[{"source":"PubMed","id":"34108458","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7DSW","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI20
Number of Residues60
DetailsTransmembrane: {"description":"Helical; Name=10","evidences":[{"source":"PubMed","id":"34108458","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7DSW","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI21
Number of Residues54
DetailsTransmembrane: {"description":"Helical; Name=11","evidences":[{"source":"PubMed","id":"34108458","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7DSW","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI22
Number of Residues48
DetailsTransmembrane: {"description":"Helical; Name=12","evidences":[{"source":"PubMed","id":"34108458","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7DSW","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI23
Number of Residues58
DetailsTransmembrane: {"description":"Helical; Name=13","evidences":[{"source":"PubMed","id":"34108458","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7DSW","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI24
Number of Residues84
DetailsRegion: {"description":"Interaction with TESC","evidences":[{"source":"PubMed","id":"30287853","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI25
Number of Residues30
DetailsRegion: {"description":"PI(4,5)P2-binding region","evidences":[{"source":"UniProtKB","id":"P26431","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI26
Number of Residues60
DetailsRegion: {"description":"Interaction with CHP2","evidences":[{"source":"PubMed","id":"21392185","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI27
Number of Residues10
DetailsRegion: {"description":"Confers pH-dependent PI(4,5)P2 binding","evidences":[{"source":"PubMed","id":"27650500","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI28
Number of Residues2
DetailsSite: {"description":"Channel pore-lining","evidences":[{"evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI29
Number of Residues2
DetailsSite: {"description":"Not glycosylated"}
ChainResidueDetails

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PDB entries from 2026-01-14

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