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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

3B8E

Crystal structure of the sodium-potassium pump

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
A0005886cellular_componentplasma membrane
A0005890cellular_componentsodium:potassium-exchanging ATPase complex
A0006813biological_processpotassium ion transport
A0006883biological_processintracellular sodium ion homeostasis
A0008556molecular_functionP-type potassium transmembrane transporter activity
A0010248biological_processestablishment or maintenance of transmembrane electrochemical gradient
A0016020cellular_componentmembrane
A0016323cellular_componentbasolateral plasma membrane
A0016887molecular_functionATP hydrolysis activity
A0030007biological_processintracellular potassium ion homeostasis
A0030424cellular_componentaxon
A0030955molecular_functionpotassium ion binding
A0031402molecular_functionsodium ion binding
A0032991cellular_componentprotein-containing complex
A0036376biological_processsodium ion export across plasma membrane
A0042383cellular_componentsarcolemma
A0042470cellular_componentmelanosome
A0051117molecular_functionATPase binding
A0055085biological_processtransmembrane transport
A0086009biological_processmembrane repolarization
A0098655biological_processmonoatomic cation transmembrane transport
A1902600biological_processproton transmembrane transport
A1990573biological_processpotassium ion import across plasma membrane
B0005890cellular_componentsodium:potassium-exchanging ATPase complex
B0006813biological_processpotassium ion transport
B0006814biological_processsodium ion transport
C0000166molecular_functionnucleotide binding
C0002028biological_processregulation of sodium ion transport
C0005215molecular_functiontransporter activity
C0005391molecular_functionP-type sodium:potassium-exchanging transporter activity
C0005515molecular_functionprotein binding
C0005524molecular_functionATP binding
C0005765cellular_componentlysosomal membrane
C0005886cellular_componentplasma membrane
C0005890cellular_componentsodium:potassium-exchanging ATPase complex
C0006813biological_processpotassium ion transport
C0006883biological_processintracellular sodium ion homeostasis
C0008556molecular_functionP-type potassium transmembrane transporter activity
C0010248biological_processestablishment or maintenance of transmembrane electrochemical gradient
C0016020cellular_componentmembrane
C0016323cellular_componentbasolateral plasma membrane
C0016887molecular_functionATP hydrolysis activity
C0030007biological_processintracellular potassium ion homeostasis
C0030424cellular_componentaxon
C0030955molecular_functionpotassium ion binding
C0031402molecular_functionsodium ion binding
C0032991cellular_componentprotein-containing complex
C0036376biological_processsodium ion export across plasma membrane
C0042383cellular_componentsarcolemma
C0042470cellular_componentmelanosome
C0051117molecular_functionATPase binding
C0055085biological_processtransmembrane transport
C0086009biological_processmembrane repolarization
C0098655biological_processmonoatomic cation transmembrane transport
C1902600biological_processproton transmembrane transport
C1990573biological_processpotassium ion import across plasma membrane
D0005890cellular_componentsodium:potassium-exchanging ATPase complex
D0006813biological_processpotassium ion transport
D0006814biological_processsodium ion transport
G0016020cellular_componentmembrane
G0043269biological_processregulation of monoatomic ion transport
G0099106molecular_functionion channel regulator activity
H0016020cellular_componentmembrane
H0043269biological_processregulation of monoatomic ion transport
H0099106molecular_functionion channel regulator activity
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG A 2002
ChainResidue
AGLY213
AASP369
ATHR371
AASP710
AMF42001
site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE RB A 2003
ChainResidue
AASP804
ATHR772
ASER775
AASN776
AGLU779
site_idAC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE RB A 2004
ChainResidue
AVAL322
AASN324
AVAL325
AGLU327
AASN776
AGLU779
AASP804
site_idAC4
Number of Residues1
DetailsBINDING SITE FOR RESIDUE RB A 2005
ChainResidue
AASP740
site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG C 2002
ChainResidue
CGLY213
CASP369
CTHR371
CASP710
CMF42001
site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE RB C 2003
ChainResidue
CTHR772
CSER775
CASN776
CGLU779
CASP804
site_idAC7
Number of Residues6
DetailsBINDING SITE FOR RESIDUE RB C 2004
ChainResidue
CVAL322
CVAL325
CGLU327
CASN776
CGLU779
CASP804
site_idAC8
Number of Residues1
DetailsBINDING SITE FOR RESIDUE RB C 2005
ChainResidue
CASP740
site_idAC9
Number of Residues13
DetailsBINDING SITE FOR RESIDUE MF4 A 2001
ChainResidue
ATHR212
AGLY213
AGLU214
AASP369
ALYS370
ATHR371
AVAL609
ATHR610
AGLY611
AASP612
ALYS691
AASN713
AMG2002
site_idBC1
Number of Residues13
DetailsBINDING SITE FOR RESIDUE MF4 C 2001
ChainResidue
CTHR212
CGLY213
CGLU214
CASP369
CLYS370
CTHR371
CVAL609
CTHR610
CGLY611
CASP612
CLYS691
CASN713
CMG2002
site_idBC2
Number of Residues1
DetailsBINDING SITE FOR RESIDUE PC1 B 1
ChainResidue
BTYR43
site_idBC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE PC1 C 1
ChainResidue
CGLY848
DTYR39
DTYR43
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues424
DetailsTransmembrane: {"description":"Helical","evidences":[{"source":"PubMed","id":"35380894","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7WYT","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues162
DetailsTopological domain: {"description":"Extracellular","evidences":[{"evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues1230
DetailsTopological domain: {"description":"Cytoplasmic","evidences":[{"evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues4
DetailsRegion: {"description":"Phosphoinositide-3 kinase binding","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues38
DetailsRegion: {"description":"Disordered","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues242
DetailsRegion: {"description":"Mediates interaction with SCN7A","evidences":[{"source":"UniProtKB","id":"Q8VDN2","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues22
DetailsCompositional bias: {"description":"Basic and acidic residues","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues2
DetailsActive site: {"description":"4-aspartylphosphate intermediate","evidences":[{"source":"UniProtKB","id":"P19156","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues28
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P05023","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"18075585","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"35380894","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3B8E","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3KDP","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7WYT","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI11
Number of Residues14
DetailsBinding site: {"evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"journal article","publicationDate":"2013","firstPage":"201","lastPage":"206","volume":"502","journal":"Nature","title":"Crystal structure of a Na1-bound Na1,K1-ATPase preceding the E1P state.","authors":["Kanai R.","Ogawa H.","Vilsen B.","Cornelius F.","Toyoshima C."]}},{"source":"PDB","id":"3WGU","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3WGV","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI12
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"journal article","publicationDate":"2013","firstPage":"201","lastPage":"206","volume":"502","journal":"Nature","title":"Crystal structure of a Na1-bound Na1,K1-ATPase preceding the E1P state.","authors":["Kanai R.","Ogawa H.","Vilsen B.","Cornelius F.","Toyoshima C."]}},{"source":"PDB","id":"3WGV","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI13
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"journal article","publicationDate":"2013","firstPage":"201","lastPage":"206","volume":"502","journal":"Nature","title":"Crystal structure of a Na1-bound Na1,K1-ATPase preceding the E1P state.","authors":["Kanai R.","Ogawa H.","Vilsen B.","Cornelius F.","Toyoshima C."]}},{"source":"PDB","id":"3WGU","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI14
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"35380894","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7WYT","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI15
Number of Residues2
DetailsBinding site: {"description":"covalent","evidences":[{"source":"UniProtKB","id":"P05023","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI16
Number of Residues8
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P06685","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI17
Number of Residues6
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"Q8VDN2","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI18
Number of Residues2
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"Q8VDN2","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI19
Number of Residues2
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"P05023","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI20
Number of Residues2
DetailsModified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"Q8VDN2","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI21
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine; by PKA","evidences":[{"source":"UniProtKB","id":"P06685","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI22
Number of Residues54
DetailsTransmembrane: {"description":"Helical; Signal-anchor for type II membrane protein","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
Catalytic Information from CSA
site_idCSA1
Number of Residues1
DetailsAnnotated By Reference To The Literature 1su4
ChainResidueDetails
AASP369
site_idCSA2
Number of Residues1
DetailsAnnotated By Reference To The Literature 1su4
ChainResidueDetails
CASP369

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PDB entries from 2026-08-26

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