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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

9ROQ

Human alpha1 Na+,K+-ATPase in the outward open E2P state

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. DpFtYDyqSLQigG
ChainResidueDetails
CASP27-GLY40
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":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"P14094","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI24
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_FI25
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_FI26
Number of Residues20
DetailsTransmembrane: {"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

258009

PDB entries from 2026-08-12

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