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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
B0016020cellular_componentmembrane
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
C0005783cellular_componentendoplasmic reticulum
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
D0005783cellular_componentendoplasmic reticulum
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
H0005794cellular_componentGolgi apparatus
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 Residues61
DetailsTRANSMEM: Helical => ECO:0000305|PubMed:32459176
ChainResidueDetails
DLYS67-MET87
DTHR99-PHE120
DGLN128-VAL148

site_idSWS_FT_FI2
Number of Residues44
DetailsTOPO_DOM: Lumenal => ECO:0000305|PubMed:32459176
ChainResidueDetails
DTYR88-PRO98
KGLN1007-VAL1013
KLYS1072-VAL1121
KARG1143-ARG1159
KGLY1262-ILE1269
KGLU1322-SER1372
KGLY1431-GLN1452
KALA1472-PHE1499
DTYR149-LEU183
KMET291-ALA350
KASN373-TRP380
KGLU544-GLU554
KGLU607-GLY615
KGLY674-PRO693
KILE716-PRO725
KGLU920-HIS931

site_idSWS_FT_FI3
Number of Residues6
DetailsTOPO_DOM: Cytoplasmic => ECO:0000305|PubMed:32459176
ChainResidueDetails
DLYS121-SER127

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569
ChainResidueDetails
DSER36
KALA1292-ASP1301
KGLU1392-PRO1409
KPRO252-LEU268
KGLY402-ASN524
KTYR576-SER586
KASN635-SER653
KASN746-THR900
KLEU953-ASN987
KLYS1033-ASN1051
KVAL1182-THR1239

site_idSWS_FT_FI5
Number of Residues20
DetailsTRANSMEM: Helical; Name=S3 of repeat I => ECO:0000250|UniProtKB:P07293
ChainResidueDetails
KALA189-SER209

site_idSWS_FT_FI6
Number of Residues18
DetailsTRANSMEM: Helical; Name=S4 of repeat I => ECO:0000250|UniProtKB:P07293
ChainResidueDetails
KVAL233-VAL251

site_idSWS_FT_FI7
Number of Residues21
DetailsTRANSMEM: Helical; Name=S5 of repeat I => ECO:0000250|UniProtKB:P07293
ChainResidueDetails
KLEU269-PHE290

site_idSWS_FT_FI8
Number of Residues80
DetailsINTRAMEM: Pore-forming => ECO:0000250|UniProtKB:P07293
ChainResidueDetails
KPHE351-VAL372
KGLN694-GLY715
KLEU1122-TYR1142
KALA1453-LEU1471

site_idSWS_FT_FI9
Number of Residues20
DetailsTRANSMEM: Helical; Name=S6 of repeat I => ECO:0000250|UniProtKB:P07293
ChainResidueDetails
KPRO381-LEU401

site_idSWS_FT_FI10
Number of Residues18
DetailsTRANSMEM: Helical; Name=S1 of repeat II => ECO:0000250|UniProtKB:P07293
ChainResidueDetails
KVAL525-SER543

site_idSWS_FT_FI11
Number of Residues20
DetailsTRANSMEM: Helical; Name=S2 of repeat II => ECO:0000250|UniProtKB:P07293
ChainResidueDetails
KVAL555-MET575

site_idSWS_FT_FI12
Number of Residues19
DetailsTRANSMEM: Helical; Name=S3 of repeat II => ECO:0000250|UniProtKB:P07293
ChainResidueDetails
KLEU587-VAL606

site_idSWS_FT_FI13
Number of Residues18
DetailsTRANSMEM: Helical; Name=S4 of repeat II => ECO:0000250|UniProtKB:P07293
ChainResidueDetails
KILE616-TRP634

site_idSWS_FT_FI14
Number of Residues19
DetailsTRANSMEM: Helical; Name=S5 of repeat II => ECO:0000250|UniProtKB:P07293
ChainResidueDetails
KLEU654-PHE673

site_idSWS_FT_FI15
Number of Residues19
DetailsTRANSMEM: Helical; Name=S6 of repeat II => ECO:0000250|UniProtKB:P07293
ChainResidueDetails
KGLY726-LEU745

site_idSWS_FT_FI16
Number of Residues18
DetailsTRANSMEM: Helical; Name=S1 of repeat III => ECO:0000250|UniProtKB:P07293
ChainResidueDetails
KILE901-ALA919

site_idSWS_FT_FI17
Number of Residues20
DetailsTRANSMEM: Helical; Name=S2 of repeat III => ECO:0000255
ChainResidueDetails
KILE932-ILE952

site_idSWS_FT_FI18
Number of Residues18
DetailsTRANSMEM: Helical; Name=S3 of repeat III => ECO:0000250|UniProtKB:P07293
ChainResidueDetails
KTYR988-ILE1006

site_idSWS_FT_FI19
Number of Residues18
DetailsTRANSMEM: Helical; Name=S4 of repeat III => ECO:0000250|UniProtKB:P07293
ChainResidueDetails
KVAL1014-ALA1032

site_idSWS_FT_FI20
Number of Residues19
DetailsTRANSMEM: Helical; Name=S5 of repeat III => ECO:0000250|UniProtKB:P07293
ChainResidueDetails
KILE1052-PHE1071

site_idSWS_FT_FI21
Number of Residues21
DetailsTRANSMEM: Helical; Name=S6 of repeat III => ECO:0000250|UniProtKB:P07293
ChainResidueDetails
KVAL1160-PHE1181

site_idSWS_FT_FI22
Number of Residues21
DetailsTRANSMEM: Helical; Name=S1 of repeat IV => ECO:0000250|UniProtKB:P07293
ChainResidueDetails
KTYR1240-TYR1261

site_idSWS_FT_FI23
Number of Residues21
DetailsTRANSMEM: Helical; Name=S2 of repeat IV => ECO:0000250|UniProtKB:P07293
ChainResidueDetails
KALA1270-ILE1291

site_idSWS_FT_FI24
Number of Residues19
DetailsTRANSMEM: Helical; Name=S3 of repeat IV => ECO:0000250|UniProtKB:P07293
ChainResidueDetails
KPRO1302-SER1321

site_idSWS_FT_FI25
Number of Residues18
DetailsTRANSMEM: Helical; Name=S4 of repeat IV => ECO:0000250|UniProtKB:P07293
ChainResidueDetails
KILE1373-GLY1391

site_idSWS_FT_FI26
Number of Residues20
DetailsTRANSMEM: Helical; Name=S5 of repeat IV => ECO:0000250|UniProtKB:P07293
ChainResidueDetails
KTYR1410-PHE1430

site_idSWS_FT_FI27
Number of Residues24
DetailsTRANSMEM: Helical; Name=S6 of repeat IV => ECO:0000250|UniProtKB:P07293
ChainResidueDetails
KALA1500-MET1524

site_idSWS_FT_FI28
Number of Residues3
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P07293
ChainResidueDetails
KGLU363
KGLU706
KGLU1135

site_idSWS_FT_FI29
Number of Residues3
DetailsSITE: Calcium ion selectivity and permeability => ECO:0000269|PubMed:8099908
ChainResidueDetails
KGLU363
KGLU1135
KGLU1464

site_idSWS_FT_FI30
Number of Residues3
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q01815
ChainResidueDetails
KSER469
KSER808
KSER815

site_idSWS_FT_FI31
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:Q01815
ChainResidueDetails
KTHR476

site_idSWS_FT_FI32
Number of Residues4
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
KASN153
KASN328
KASN1436
KASN1487

226707

PDB entries from 2024-10-30

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