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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

8J0O

cryo-EM structure of human EMC and VDAC

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
E0000139cellular_componentGolgi membrane
E0005515molecular_functionprotein binding
E0005737cellular_componentcytoplasm
E0005769cellular_componentearly endosome
E0005789cellular_componentendoplasmic reticulum membrane
E0005794cellular_componentGolgi apparatus
E0005886cellular_componentplasma membrane
E0006824biological_processcobalt ion transport
E0015087molecular_functioncobalt ion transmembrane transporter activity
E0015093molecular_functionferrous iron transmembrane transporter activity
E0015095molecular_functionmagnesium ion transmembrane transporter activity
E0015693biological_processmagnesium ion transport
E0016020cellular_componentmembrane
E0022857molecular_functiontransmembrane transporter activity
E0031901cellular_componentearly endosome membrane
E0032977molecular_functionmembrane insertase activity
E0034755biological_processiron ion transmembrane transport
E0045050biological_processprotein insertion into ER membrane by stop-transfer membrane-anchor sequence
E0055085biological_processtransmembrane transport
E0071816biological_processtail-anchored membrane protein insertion into ER membrane
E0072546cellular_componentEMC complex
E1903830biological_processmagnesium ion transmembrane transport
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
K0000166molecular_functionnucleotide binding
K0005244molecular_functionvoltage-gated monoatomic ion channel activity
K0005515molecular_functionprotein binding
K0005524molecular_functionATP binding
K0005634cellular_componentnucleus
K0005739cellular_componentmitochondrion
K0005741cellular_componentmitochondrial outer membrane
K0005757cellular_componentmitochondrial permeability transition pore complex
K0005886cellular_componentplasma membrane
K0006811biological_processmonoatomic ion transport
K0006820biological_processmonoatomic anion transport
K0006869biological_processlipid transport
K0006915biological_processapoptotic process
K0008142molecular_functionoxysterol binding
K0008289molecular_functionlipid binding
K0008308molecular_functionvoltage-gated monoatomic anion channel activity
K0015288molecular_functionporin activity
K0015485molecular_functioncholesterol binding
K0016020cellular_componentmembrane
K0019901molecular_functionprotein kinase binding
K0030855biological_processepithelial cell differentiation
K0031210molecular_functionphosphatidylcholine binding
K0031966cellular_componentmitochondrial membrane
K0036444biological_processcalcium import into the mitochondrion
K0042645cellular_componentmitochondrial nucleoid
K0042802molecular_functionidentical protein binding
K0042866biological_processpyruvate biosynthetic process
K0043066biological_processnegative regulation of apoptotic process
K0044325molecular_functiontransmembrane transporter binding
K0045121cellular_componentmembrane raft
K0046930cellular_componentpore complex
K0055085biological_processtransmembrane transport
K0070062cellular_componentextracellular exosome
K0097001molecular_functionceramide binding
K0098656biological_processmonoatomic anion transmembrane transport
K0110099biological_processnegative regulation of calcium import into the mitochondrion
K1901524biological_processregulation of mitophagy
K1901526biological_processpositive regulation of mitophagy
K1903146biological_processregulation of autophagy of mitochondrion
K1905091biological_processpositive regulation of type 2 mitophagy
K1990542biological_processmitochondrial transmembrane transport
K2000378biological_processnegative regulation of reactive oxygen species metabolic process
Functional Information from PROSITE/UniProt
site_idPS00558
Number of Residues23
DetailsEUKARYOTIC_PORIN Eukaryotic mitochondrial porin signature. YqiDPdAcfsAKVNNssliGLgY
ChainResidueDetails
KTYR225-TYR247
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 Residues174
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":"N-acetylalanine","evidences":[{"source":"PubMed","id":"22814378","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues1
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues65
DetailsTopological domain: {"description":"Lumenal","evidences":[{"source":"PubMed","id":"32439656","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI11
Number of Residues61
DetailsTransmembrane: {"description":"Helical","evidences":[{"source":"PubMed","id":"32459176","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI12
Number of Residues44
DetailsTopological domain: {"description":"Lumenal","evidences":[{"source":"PubMed","id":"32459176","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI13
Number of Residues6
DetailsTopological domain: {"description":"Cytoplasmic","evidences":[{"source":"PubMed","id":"32459176","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI14
Number of Residues20
DetailsTransmembrane: {"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI15
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_FI16
Number of Residues164
DetailsTransmembrane: {"description":"Beta stranded","evidences":[{"source":"PubMed","id":"18755977","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18832158","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI17
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"Q60932","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI18
Number of Residues6
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"18755977","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI19
Number of Residues1
DetailsSite: {"description":"Involved in ceramide and phosphatidylcholine binding. Critical for channel structural stability and gating","evidences":[{"source":"PubMed","id":"31015432","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18832158","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI20
Number of Residues1
DetailsModified residue: {"description":"N-acetylalanine","evidences":[{"source":"PubMed","id":"2559745","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"MAR-2005","submissionDatabase":"UniProtKB","authors":["Bienvenut W.V."]}},{"source":"PubMed","id":"19413330","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"22223895","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"22814378","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"25944712","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI21
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"Q9Z2L0","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI22
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"Q60932","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI23
Number of Residues1
DetailsModified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"Q60932","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI24
Number of Residues1
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"Q60932","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI25
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI26
Number of Residues1
DetailsModified residue: {"description":"N6-acetyllysine; alternate","evidences":[{"source":"UniProtKB","id":"Q60932","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI27
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine; by NEK1","evidences":[{"source":"PubMed","id":"20230784","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI28
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI29
Number of Residues1
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"Q60932","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI30
Number of Residues1
DetailsModified residue: {"description":"N6-acetyllysine; alternate","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI31
Number of Residues1
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"source":"PubMed","id":"32047033","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI32
Number of Residues4
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"source":"PubMed","id":"25621951","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"32047033","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI33
Number of Residues1
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate","evidences":[{"source":"PubMed","id":"32047033","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI34
Number of Residues2
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"source":"PubMed","id":"25621951","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI35
Number of Residues1
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate","evidences":[{"source":"PubMed","id":"25621951","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"32047033","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI36
Number of Residues1
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate","evidences":[{"source":"PubMed","id":"25621951","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

246704

PDB entries from 2025-12-24

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