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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

8EOI

Structure of a human EMC:human Cav1.2 channel complex in GDN detergent

Functional Information from GO Data
ChainGOidnamespacecontents
A0072546cellular_componentEMC complex
B0005515molecular_functionprotein binding
B0005737cellular_componentcytoplasm
B0005783cellular_componentendoplasmic reticulum
B0005789cellular_componentendoplasmic reticulum membrane
B0032977molecular_functionmembrane insertase activity
B0042406cellular_componentextrinsic component of endoplasmic reticulum membrane
B0045050biological_processprotein insertion into ER membrane by stop-transfer membrane-anchor sequence
B0071816biological_processtail-anchored membrane protein insertion into ER membrane
B0072546cellular_componentEMC complex
C0005515molecular_functionprotein binding
C0005789cellular_componentendoplasmic reticulum membrane
C0016020cellular_componentmembrane
C0032977molecular_functionmembrane insertase activity
C0045050biological_processprotein insertion into ER membrane by stop-transfer membrane-anchor sequence
C0071816biological_processtail-anchored membrane protein insertion into ER membrane
C0072546cellular_componentEMC complex
D0005515molecular_functionprotein binding
D0005789cellular_componentendoplasmic reticulum membrane
D0006915biological_processapoptotic process
D0016020cellular_componentmembrane
D0032977molecular_functionmembrane insertase activity
D0045050biological_processprotein insertion into ER membrane by stop-transfer membrane-anchor sequence
D0071816biological_processtail-anchored membrane protein insertion into ER membrane
D0072546cellular_componentEMC complex
F0000045biological_processautophagosome assembly
F0005515molecular_functionprotein binding
F0005783cellular_componentendoplasmic reticulum
F0005789cellular_componentendoplasmic reticulum membrane
F0016020cellular_componentmembrane
F0032977molecular_functionmembrane insertase activity
F0045050biological_processprotein insertion into ER membrane by stop-transfer membrane-anchor sequence
F0071816biological_processtail-anchored membrane protein insertion into ER membrane
F0072546cellular_componentEMC complex
F1903349cellular_componentomegasome membrane
G0030246molecular_functioncarbohydrate binding
H0005515molecular_functionprotein binding
H0005737cellular_componentcytoplasm
H0005783cellular_componentendoplasmic reticulum
H0005789cellular_componentendoplasmic reticulum membrane
H0016020cellular_componentmembrane
H0032977molecular_functionmembrane insertase activity
H0045050biological_processprotein insertion into ER membrane by stop-transfer membrane-anchor sequence
H0071816biological_processtail-anchored membrane protein insertion into ER membrane
H0072546cellular_componentEMC complex
J0005245molecular_functionvoltage-gated calcium channel activity
J0005891cellular_componentvoltage-gated calcium channel complex
J0070588biological_processcalcium ion transmembrane transport
K0005216molecular_functionmonoatomic ion channel activity
K0005245molecular_functionvoltage-gated calcium channel activity
K0005891cellular_componentvoltage-gated calcium channel complex
K0006811biological_processmonoatomic ion transport
K0016020cellular_componentmembrane
K0055085biological_processtransmembrane transport
K0070588biological_processcalcium ion transmembrane transport
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues164
DetailsTransmembrane: {"description":"Helical","evidences":[{"source":"PubMed","id":"32439656","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues26
DetailsTopological domain: {"description":"Cytoplasmic","evidences":[{"source":"PubMed","id":"32439656","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues2
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"32439656","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6WW7","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"32439656","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6WW7","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues33
DetailsRepeat: {"description":"TPR 1","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues33
DetailsRepeat: {"description":"TPR 2","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues33
DetailsRepeat: {"description":"TPR 3","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues1
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues65
DetailsTopological domain: {"description":"Lumenal","evidences":[{"source":"PubMed","id":"32439656","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"32439656","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI11
Number of Residues18
DetailsTransmembrane: {"description":"Helical; Name=S1 of repeat I","evidences":[{"source":"UniProtKB","id":"P07293","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI12
Number of Residues181
DetailsTopological domain: {"description":"Extracellular","evidences":[{"evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI13
Number of Residues20
DetailsTransmembrane: {"description":"Helical; Name=S2 of repeat I","evidences":[{"source":"UniProtKB","id":"P07293","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI14
Number of Residues144
DetailsTopological domain: {"description":"Cytoplasmic","evidences":[{"evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI15
Number of Residues20
DetailsTransmembrane: {"description":"Helical; Name=S3 of repeat I","evidences":[{"source":"UniProtKB","id":"P07293","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI16
Number of Residues21
DetailsTransmembrane: {"description":"Helical; Name=S5 of repeat I","evidences":[{"source":"UniProtKB","id":"P07293","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI17
Number of Residues80
DetailsIntramembrane: {"description":"Pore-forming","evidences":[{"source":"UniProtKB","id":"P07293","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI18
Number of Residues20
DetailsTransmembrane: {"description":"Helical; Name=S6 of repeat I","evidences":[{"source":"UniProtKB","id":"P07293","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI19
Number of Residues18
DetailsTransmembrane: {"description":"Helical; Name=S1 of repeat II","evidences":[{"source":"UniProtKB","id":"P07293","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI20
Number of Residues20
DetailsTransmembrane: {"description":"Helical; Name=S2 of repeat II","evidences":[{"source":"UniProtKB","id":"P07293","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI21
Number of Residues19
DetailsTransmembrane: {"description":"Helical; Name=S3 of repeat II","evidences":[{"source":"UniProtKB","id":"P07293","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI22
Number of Residues18
DetailsTransmembrane: {"description":"Helical; Name=S4 of repeat II","evidences":[{"source":"UniProtKB","id":"P07293","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI23
Number of Residues19
DetailsTransmembrane: {"description":"Helical; Name=S5 of repeat II","evidences":[{"source":"UniProtKB","id":"P07293","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI24
Number of Residues19
DetailsTransmembrane: {"description":"Helical; Name=S6 of repeat II","evidences":[{"source":"UniProtKB","id":"P07293","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI25
Number of Residues19
DetailsTransmembrane: {"description":"Helical; Name=S5 of repeat III","evidences":[{"source":"UniProtKB","id":"P07293","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI26
Number of Residues21
DetailsTransmembrane: {"description":"Helical; Name=S6 of repeat III","evidences":[{"source":"UniProtKB","id":"P07293","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI27
Number of Residues21
DetailsTransmembrane: {"description":"Helical; Name=S1 of repeat IV","evidences":[{"source":"UniProtKB","id":"P07293","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI28
Number of Residues21
DetailsTransmembrane: {"description":"Helical; Name=S2 of repeat IV","evidences":[{"source":"UniProtKB","id":"P07293","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI29
Number of Residues18
DetailsTransmembrane: {"description":"Helical; Name=S4 of repeat IV","evidences":[{"source":"UniProtKB","id":"P07293","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI30
Number of Residues20
DetailsTransmembrane: {"description":"Helical; Name=S5 of repeat IV","evidences":[{"source":"UniProtKB","id":"P07293","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI31
Number of Residues24
DetailsTransmembrane: {"description":"Helical; Name=S6 of repeat IV","evidences":[{"source":"UniProtKB","id":"P07293","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI32
Number of Residues246
DetailsRepeat: {"description":"II"}
ChainResidueDetails
site_idSWS_FT_FI33
Number of Residues17
DetailsRegion: {"description":"AID/alpha-interaction domain; mediates interaction with the beta subunit","evidences":[{"source":"PubMed","id":"15141227","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI34
Number of Residues68
DetailsRegion: {"description":"Dihydropyridine binding","evidences":[{"source":"UniProtKB","id":"P07293","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI35
Number of Residues42
DetailsRegion: {"description":"Phenylalkylamine binding","evidences":[{"source":"UniProtKB","id":"P07293","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI36
Number of Residues3
DetailsMotif: {"description":"Selectivity filter of repeat I","evidences":[{"source":"UniProtKB","id":"P07293","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI37
Number of Residues3
DetailsMotif: {"description":"Selectivity filter of repeat II","evidences":[{"source":"UniProtKB","id":"P07293","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI38
Number of Residues3
DetailsMotif: {"description":"Selectivity filter of repeat III","evidences":[{"source":"UniProtKB","id":"P07293","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI39
Number of Residues3
DetailsMotif: {"description":"Selectivity filter of repeat IV","evidences":[{"source":"UniProtKB","id":"P07293","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI40
Number of Residues3
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P07293","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI41
Number of Residues3
DetailsSite: {"description":"Calcium ion selectivity and permeability","evidences":[{"source":"PubMed","id":"8099908","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI42
Number of Residues4
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI43
Number of Residues69
DetailsDomain: {"description":"SH3","evidences":[{"source":"PROSITE-ProRule","id":"PRU00192","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI44
Number of Residues150
DetailsRegion: {"description":"Mediates interaction with the alpha subunit","evidences":[{"source":"UniProtKB","id":"P54287","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

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PDB entries from 2025-12-24

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