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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

7E20

Cryo EM structure of a K+-bound Na+,K+-ATPase in the E2 state

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0002028biological_processregulation of sodium ion transport
A0005215molecular_functiontransporter activity
A0005391molecular_functionP-type sodium:potassium-exchanging transporter activity
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0005765cellular_componentlysosomal membrane
A0005783cellular_componentendoplasmic reticulum
A0005794cellular_componentGolgi apparatus
A0005886cellular_componentplasma membrane
A0005890cellular_componentsodium:potassium-exchanging ATPase complex
A0006813biological_processpotassium ion transport
A0006883biological_processintracellular sodium ion homeostasis
A0007231biological_processosmosensory signaling pathway
A0008556molecular_functionP-type potassium transmembrane transporter activity
A0010248biological_processestablishment or maintenance of transmembrane electrochemical gradient
A0014069cellular_componentpostsynaptic density
A0016020cellular_componentmembrane
A0016323cellular_componentbasolateral plasma membrane
A0016324cellular_componentapical plasma membrane
A0016328cellular_componentlateral plasma membrane
A0016791molecular_functionphosphatase activity
A0016887molecular_functionATP hydrolysis activity
A0030007biological_processintracellular potassium ion homeostasis
A0030315cellular_componentT-tubule
A0030424cellular_componentaxon
A0030955molecular_functionpotassium ion binding
A0031402molecular_functionsodium ion binding
A0032991cellular_componentprotein-containing complex
A0035725biological_processsodium ion transmembrane transport
A0036126cellular_componentsperm flagellum
A0036376biological_processsodium ion export across plasma membrane
A0042383cellular_componentsarcolemma
A0042470cellular_componentmelanosome
A0044325molecular_functiontransmembrane transporter binding
A0045121cellular_componentmembrane raft
A0051087molecular_functionprotein-folding chaperone binding
A0055078biological_processsodium ion homeostasis
A0055119biological_processrelaxation of cardiac muscle
A0060342cellular_componentphotoreceptor inner segment membrane
A0070062cellular_componentextracellular exosome
A0071383biological_processcellular response to steroid hormone stimulus
A0071805biological_processpotassium ion transmembrane transport
A0086002biological_processcardiac muscle cell action potential involved in contraction
A0086009biological_processmembrane repolarization
A0086013biological_processmembrane repolarization during cardiac muscle cell action potential
A0086064biological_processcell communication by electrical coupling involved in cardiac conduction
A1902600biological_processproton transmembrane transport
A1903416biological_processresponse to glycoside
A1903561cellular_componentextracellular vesicle
A1990239molecular_functionsteroid hormone binding
A1990573biological_processpotassium ion import across plasma membrane
B0001666biological_processresponse to hypoxia
B0001671molecular_functionATPase activator activity
B0005391molecular_functionP-type sodium:potassium-exchanging transporter activity
B0005515molecular_functionprotein binding
B0005765cellular_componentlysosomal membrane
B0005886cellular_componentplasma membrane
B0005890cellular_componentsodium:potassium-exchanging ATPase complex
B0005901cellular_componentcaveola
B0006813biological_processpotassium ion transport
B0006814biological_processsodium ion transport
B0006874biological_processintracellular calcium ion homeostasis
B0006883biological_processintracellular sodium ion homeostasis
B0010248biological_processestablishment or maintenance of transmembrane electrochemical gradient
B0010468biological_processregulation of gene expression
B0010882biological_processregulation of cardiac muscle contraction by calcium ion signaling
B0014704cellular_componentintercalated disc
B0016020cellular_componentmembrane
B0016323cellular_componentbasolateral plasma membrane
B0016324cellular_componentapical plasma membrane
B0016328cellular_componentlateral plasma membrane
B0019901molecular_functionprotein kinase binding
B0023026molecular_functionMHC class II protein complex binding
B0030001biological_processmetal ion transport
B0030007biological_processintracellular potassium ion homeostasis
B0030315cellular_componentT-tubule
B0030674molecular_functionprotein-macromolecule adaptor activity
B0035725biological_processsodium ion transmembrane transport
B0036126cellular_componentsperm flagellum
B0036376biological_processsodium ion export across plasma membrane
B0042383cellular_componentsarcolemma
B0044861biological_processprotein transport into plasma membrane raft
B0046034biological_processATP metabolic process
B0046982molecular_functionprotein heterodimerization activity
B0050821biological_processprotein stabilization
B0051117molecular_functionATPase binding
B0055119biological_processrelaxation of cardiac muscle
B0060048biological_processcardiac muscle contraction
B0070062cellular_componentextracellular exosome
B0072659biological_processprotein localization to plasma membrane
B0086009biological_processmembrane repolarization
B0086013biological_processmembrane repolarization during cardiac muscle cell action potential
B0086064biological_processcell communication by electrical coupling involved in cardiac conduction
B0141109molecular_functiontransporter activator activity
B1902600biological_processproton transmembrane transport
B1903169biological_processregulation of calcium ion transmembrane transport
B1903278biological_processpositive regulation of sodium ion export across plasma membrane
B1903288biological_processpositive regulation of potassium ion import across plasma membrane
B1903561cellular_componentextracellular vesicle
B1990573biological_processpotassium ion import across plasma membrane
C0001671molecular_functionATPase activator activity
C0005886cellular_componentplasma membrane
C0005890cellular_componentsodium:potassium-exchanging ATPase complex
C0006811biological_processmonoatomic ion transport
C0006812biological_processmonoatomic cation transport
C0008285biological_processnegative regulation of cell population proliferation
C0010248biological_processestablishment or maintenance of transmembrane electrochemical gradient
C0016020cellular_componentmembrane
C0016323cellular_componentbasolateral plasma membrane
C0017080molecular_functionsodium channel regulator activity
C0030674molecular_functionprotein-macromolecule adaptor activity
C0036376biological_processsodium ion export across plasma membrane
C0043269biological_processregulation of monoatomic ion transport
C0055085biological_processtransmembrane transport
C0070062cellular_componentextracellular exosome
C0071475biological_processcellular hyperosmotic salinity response
C0099106molecular_functionion channel regulator activity
C1902600biological_processproton transmembrane transport
C1903278biological_processpositive regulation of sodium ion export across plasma membrane
C1990573biological_processpotassium ion import across plasma membrane
Functional Information from PROSITE/UniProt
site_idPS00390
Number of Residues21
DetailsATPASE_NA_K_BETA_1 Sodium and potassium ATPases beta subunits signature 1. WkkFiWNsekkefLGRTggsW
ChainResidueDetails
BTRP12-TRP32
site_idPS00391
Number of Residues16
DetailsATPASE_NA_K_BETA_2 Sodium and potassium ATPases beta subunits signature 2. RkvCRfklewLgnCSG
ChainResidueDetails
BARG146-GLY161
site_idPS01310
Number of Residues14
DetailsFXYD FXYD family signature. DpFyYDyeTVRngG
ChainResidueDetails
CASP17-GLY30
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues191
DetailsTransmembrane: {"description":"Helical","evidences":[{"source":"PubMed","id":"35803952","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7E20","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues81
DetailsTopological domain: {"description":"Extracellular","evidences":[{"evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues617
DetailsTopological domain: {"description":"Cytoplasmic","evidences":[{"evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues23
DetailsTransmembrane: {"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"35803952","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7E20","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues2
DetailsRegion: {"description":"Phosphoinositide-3 kinase binding","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues19
DetailsRegion: {"description":"Disordered","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues121
DetailsRegion: {"description":"Mediates interaction with SCN7A","evidences":[{"source":"UniProtKB","id":"Q8VDN2","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues1
DetailsActive site: {"description":"4-aspartylphosphate intermediate","evidences":[{"source":"UniProtKB","id":"P19156","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues14
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"35803952","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7E20","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues3
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"35803952","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"NOV-2024","submissionDatabase":"PDB data bank","title":"Structural basis of a sodium pump quaternary complex leading phospholipid scrambling in the living cell.","authors":["Dou Y.","Abe K.","Suzuki J."]}},{"source":"PDB","id":"7E20","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"9KCI","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"9KCK","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI11
Number of Residues9
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P05024","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI12
Number of Residues1
DetailsBinding site: {"evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"NOV-2024","submissionDatabase":"PDB data bank","title":"Structural basis of a sodium pump quaternary complex leading phospholipid scrambling in the living cell.","authors":["Dou Y.","Abe K.","Suzuki J."]}},{"source":"PDB","id":"9KCG","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI13
Number of Residues1
DetailsBinding site: {"description":"covalent","evidences":[{"source":"PubMed","id":"35803952","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7E20","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI14
Number of Residues4
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P06685","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI15
Number of Residues3
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"Q8VDN2","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI16
Number of Residues1
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"Q8VDN2","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI17
Number of Residues1
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"19690332","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI18
Number of Residues1
DetailsModified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"Q8VDN2","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI19
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine; by PKA","evidences":[{"source":"UniProtKB","id":"P06685","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI20
Number of Residues27
DetailsTransmembrane: {"description":"Helical; Signal-anchor for type II membrane protein","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI21
Number of Residues240
DetailsTopological domain: {"description":"Extracellular","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI22
Number of Residues112
DetailsRegion: {"description":"immunoglobulin-like"}
ChainResidueDetails
site_idSWS_FT_FI23
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P07340","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI24
Number of Residues1
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"P14094","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI25
Number of Residues2
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"12754519","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI26
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"12754519","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19349973","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI27
Number of Residues17
DetailsTransmembrane: {"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

256158

PDB entries from 2026-07-08

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