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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

6K7N

Cryo-EM structure of the human P4-type flippase ATP8A1-CDC50 (E1P state)

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0000287molecular_functionmagnesium ion binding
A0005215molecular_functiontransporter activity
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0005783cellular_componentendoplasmic reticulum
A0005794cellular_componentGolgi apparatus
A0005802cellular_componenttrans-Golgi network
A0005829cellular_componentcytosol
A0005886cellular_componentplasma membrane
A0006869biological_processlipid transport
A0007612biological_processlearning
A0012505cellular_componentendomembrane system
A0015914biological_processphospholipid transport
A0016020cellular_componentmembrane
A0016887molecular_functionATP hydrolysis activity
A0019829molecular_functionATPase-coupled monoatomic cation transmembrane transporter activity
A0030335biological_processpositive regulation of cell migration
A0030659cellular_componentcytoplasmic vesicle membrane
A0030672cellular_componentsynaptic vesicle membrane
A0031090cellular_componentorganelle membrane
A0031410cellular_componentcytoplasmic vesicle
A0034220biological_processmonoatomic ion transmembrane transport
A0035577cellular_componentazurophil granule membrane
A0035579cellular_componentspecific granule membrane
A0042584cellular_componentchromaffin granule membrane
A0045202cellular_componentsynapse
A0045332biological_processphospholipid translocation
A0046872molecular_functionmetal ion binding
A0048488biological_processsynaptic vesicle endocytosis
A0061092biological_processpositive regulation of phospholipid translocation
A0070062cellular_componentextracellular exosome
A0090556molecular_functionphosphatidylserine floppase activity
A0098588cellular_componentbounding membrane of organelle
A0098655biological_processmonoatomic cation transmembrane transport
A0098978cellular_componentglutamatergic synapse
A0099503cellular_componentsecretory vesicle
A0140326molecular_functionATPase-coupled intramembrane lipid transporter activity
A0140331biological_processaminophospholipid translocation
A0140346molecular_functionphosphatidylserine flippase activity
A0150104biological_processtransport across blood-brain barrier
A1990531cellular_componentphospholipid-translocating ATPase complex
C0005198molecular_functionstructural molecule activity
C0005515molecular_functionprotein binding
C0005783cellular_componentendoplasmic reticulum
C0005794cellular_componentGolgi apparatus
C0005886cellular_componentplasma membrane
C0006855biological_processxenobiotic transmembrane transport
C0006869biological_processlipid transport
C0010976biological_processpositive regulation of neuron projection development
C0015247molecular_functionaminophospholipid flippase activity
C0015917biological_processaminophospholipid transport
C0016020cellular_componentmembrane
C0016324cellular_componentapical plasma membrane
C0030658cellular_componenttransport vesicle membrane
C0031410cellular_componentcytoplasmic vesicle
C0031901cellular_componentearly endosome membrane
C0031902cellular_componentlate endosome membrane
C0035577cellular_componentazurophil granule membrane
C0035579cellular_componentspecific granule membrane
C0036010biological_processprotein localization to endosome
C0045332biological_processphospholipid translocation
C0061092biological_processpositive regulation of phospholipid translocation
C0070863biological_processpositive regulation of protein exit from endoplasmic reticulum
C0140331biological_processaminophospholipid translocation
C1990531cellular_componentphospholipid-translocating ATPase complex
Functional Information from PROSITE/UniProt
site_idPS00154
Number of Residues7
DetailsATPASE_E1_E2 E1-E2 ATPases phosphorylation site. DKTGTLT
ChainResidueDetails
AASP409-THR415
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI4
Number of Residues1
DetailsActive site: {"description":"4-aspartylphosphate intermediate","evidences":[{"source":"PubMed","id":"31416931","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues6
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"31416931","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues8
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P04191","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues1
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"Q8NB49","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues251
DetailsTransmembrane: {"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues324
DetailsTopological domain: {"description":"Exoplasmic loop","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues34
DetailsTopological domain: {"description":"Cytoplasmic","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI11
Number of Residues7
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI12
Number of Residues1
DetailsSite: {"description":"Involved in the recognition of the lipid substrate on the exoplasmic side","evidences":[{"source":"UniProtKB","id":"C7EXK4","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI13
Number of Residues1
DetailsSite: {"description":"Involved in the release of the transported lipid into the cytosolic leaflet","evidences":[{"source":"UniProtKB","id":"C7EXK4","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI14
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"31416931","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6K7G","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6K7H","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6K7I","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6K7J","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6K7K","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6K7L","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6K7M","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI15
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"31416931","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6K7G","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6K7H","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6K7I","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6K7J","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6K7K","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6K7L","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6K7M","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI16
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"19349973","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI17
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"31416931","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6K7G","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6K7H","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6K7I","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6K7J","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6K7K","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6K7L","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6K7M","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

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PDB entries from 2025-07-23

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