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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

6G73

The dynamic nature of the VDAC1 channels in bilayers: human VDAC1 at 3.3 Angstrom resolution

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0005244molecular_functionvoltage-gated monoatomic ion channel activity
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0005634cellular_componentnucleus
A0005739cellular_componentmitochondrion
A0005741cellular_componentmitochondrial outer membrane
A0005757cellular_componentmitochondrial permeability transition pore complex
A0005886cellular_componentplasma membrane
A0006811biological_processmonoatomic ion transport
A0006820biological_processmonoatomic anion transport
A0006869biological_processlipid transport
A0006915biological_processapoptotic process
A0008142molecular_functionoxysterol binding
A0008289molecular_functionlipid binding
A0008308molecular_functionvoltage-gated monoatomic anion channel activity
A0015288molecular_functionporin activity
A0015485molecular_functioncholesterol binding
A0016020cellular_componentmembrane
A0019901molecular_functionprotein kinase binding
A0030855biological_processepithelial cell differentiation
A0031210molecular_functionphosphatidylcholine binding
A0031966cellular_componentmitochondrial membrane
A0036444biological_processcalcium import into the mitochondrion
A0042645cellular_componentmitochondrial nucleoid
A0042802molecular_functionidentical protein binding
A0042866biological_processpyruvate biosynthetic process
A0043066biological_processnegative regulation of apoptotic process
A0044325molecular_functiontransmembrane transporter binding
A0045121cellular_componentmembrane raft
A0046930cellular_componentpore complex
A0055085biological_processtransmembrane transport
A0070062cellular_componentextracellular exosome
A0097001molecular_functionceramide binding
A0098656biological_processmonoatomic anion transmembrane transport
A0110099biological_processnegative regulation of calcium import into the mitochondrion
A1901524biological_processregulation of mitophagy
A1901526biological_processpositive regulation of mitophagy
A1903146biological_processregulation of autophagy of mitochondrion
A1905091biological_processpositive regulation of type 2 mitophagy
A1990542biological_processmitochondrial transmembrane transport
A2000378biological_processnegative regulation of reactive oxygen species metabolic process
B0000166molecular_functionnucleotide binding
B0005244molecular_functionvoltage-gated monoatomic ion channel activity
B0005515molecular_functionprotein binding
B0005524molecular_functionATP binding
B0005634cellular_componentnucleus
B0005739cellular_componentmitochondrion
B0005741cellular_componentmitochondrial outer membrane
B0005757cellular_componentmitochondrial permeability transition pore complex
B0005886cellular_componentplasma membrane
B0006811biological_processmonoatomic ion transport
B0006820biological_processmonoatomic anion transport
B0006869biological_processlipid transport
B0006915biological_processapoptotic process
B0008142molecular_functionoxysterol binding
B0008289molecular_functionlipid binding
B0008308molecular_functionvoltage-gated monoatomic anion channel activity
B0015288molecular_functionporin activity
B0015485molecular_functioncholesterol binding
B0016020cellular_componentmembrane
B0019901molecular_functionprotein kinase binding
B0030855biological_processepithelial cell differentiation
B0031210molecular_functionphosphatidylcholine binding
B0031966cellular_componentmitochondrial membrane
B0036444biological_processcalcium import into the mitochondrion
B0042645cellular_componentmitochondrial nucleoid
B0042802molecular_functionidentical protein binding
B0042866biological_processpyruvate biosynthetic process
B0043066biological_processnegative regulation of apoptotic process
B0044325molecular_functiontransmembrane transporter binding
B0045121cellular_componentmembrane raft
B0046930cellular_componentpore complex
B0055085biological_processtransmembrane transport
B0070062cellular_componentextracellular exosome
B0097001molecular_functionceramide binding
B0098656biological_processmonoatomic anion transmembrane transport
B0110099biological_processnegative regulation of calcium import into the mitochondrion
B1901524biological_processregulation of mitophagy
B1901526biological_processpositive regulation of mitophagy
B1903146biological_processregulation of autophagy of mitochondrion
B1905091biological_processpositive regulation of type 2 mitophagy
B1990542biological_processmitochondrial transmembrane transport
B2000378biological_processnegative regulation of reactive oxygen species metabolic process
C0000166molecular_functionnucleotide binding
C0005244molecular_functionvoltage-gated monoatomic ion channel activity
C0005515molecular_functionprotein binding
C0005524molecular_functionATP binding
C0005634cellular_componentnucleus
C0005739cellular_componentmitochondrion
C0005741cellular_componentmitochondrial outer membrane
C0005757cellular_componentmitochondrial permeability transition pore complex
C0005886cellular_componentplasma membrane
C0006811biological_processmonoatomic ion transport
C0006820biological_processmonoatomic anion transport
C0006869biological_processlipid transport
C0006915biological_processapoptotic process
C0008142molecular_functionoxysterol binding
C0008289molecular_functionlipid binding
C0008308molecular_functionvoltage-gated monoatomic anion channel activity
C0015288molecular_functionporin activity
C0015485molecular_functioncholesterol binding
C0016020cellular_componentmembrane
C0019901molecular_functionprotein kinase binding
C0030855biological_processepithelial cell differentiation
C0031210molecular_functionphosphatidylcholine binding
C0031966cellular_componentmitochondrial membrane
C0036444biological_processcalcium import into the mitochondrion
C0042645cellular_componentmitochondrial nucleoid
C0042802molecular_functionidentical protein binding
C0042866biological_processpyruvate biosynthetic process
C0043066biological_processnegative regulation of apoptotic process
C0044325molecular_functiontransmembrane transporter binding
C0045121cellular_componentmembrane raft
C0046930cellular_componentpore complex
C0055085biological_processtransmembrane transport
C0070062cellular_componentextracellular exosome
C0097001molecular_functionceramide binding
C0098656biological_processmonoatomic anion transmembrane transport
C0110099biological_processnegative regulation of calcium import into the mitochondrion
C1901524biological_processregulation of mitophagy
C1901526biological_processpositive regulation of mitophagy
C1903146biological_processregulation of autophagy of mitochondrion
C1905091biological_processpositive regulation of type 2 mitophagy
C1990542biological_processmitochondrial transmembrane transport
C2000378biological_processnegative regulation of reactive oxygen species metabolic process
D0000166molecular_functionnucleotide binding
D0005244molecular_functionvoltage-gated monoatomic ion channel activity
D0005515molecular_functionprotein binding
D0005524molecular_functionATP binding
D0005634cellular_componentnucleus
D0005739cellular_componentmitochondrion
D0005741cellular_componentmitochondrial outer membrane
D0005757cellular_componentmitochondrial permeability transition pore complex
D0005886cellular_componentplasma membrane
D0006811biological_processmonoatomic ion transport
D0006820biological_processmonoatomic anion transport
D0006869biological_processlipid transport
D0006915biological_processapoptotic process
D0008142molecular_functionoxysterol binding
D0008289molecular_functionlipid binding
D0008308molecular_functionvoltage-gated monoatomic anion channel activity
D0015288molecular_functionporin activity
D0015485molecular_functioncholesterol binding
D0016020cellular_componentmembrane
D0019901molecular_functionprotein kinase binding
D0030855biological_processepithelial cell differentiation
D0031210molecular_functionphosphatidylcholine binding
D0031966cellular_componentmitochondrial membrane
D0036444biological_processcalcium import into the mitochondrion
D0042645cellular_componentmitochondrial nucleoid
D0042802molecular_functionidentical protein binding
D0042866biological_processpyruvate biosynthetic process
D0043066biological_processnegative regulation of apoptotic process
D0044325molecular_functiontransmembrane transporter binding
D0045121cellular_componentmembrane raft
D0046930cellular_componentpore complex
D0055085biological_processtransmembrane transport
D0070062cellular_componentextracellular exosome
D0097001molecular_functionceramide binding
D0098656biological_processmonoatomic anion transmembrane transport
D0110099biological_processnegative regulation of calcium import into the mitochondrion
D1901524biological_processregulation of mitophagy
D1901526biological_processpositive regulation of mitophagy
D1903146biological_processregulation of autophagy of mitochondrion
D1905091biological_processpositive regulation of type 2 mitophagy
D1990542biological_processmitochondrial transmembrane transport
D2000378biological_processnegative regulation of reactive oxygen species metabolic process
Functional Information from PDB Data
site_idAC1
Number of Residues2
Detailsbinding site for residue MC3 A 301
ChainResidue
ATRP149
ATYR173
site_idAC2
Number of Residues1
Detailsbinding site for residue MC3 A 302
ChainResidue
APHE190
site_idAC3
Number of Residues3
Detailsbinding site for residue MC3 B 301
ChainResidue
BALA92
BARG93
CPHE190
site_idAC4
Number of Residues2
Detailsbinding site for residue MC3 B 302
ChainResidue
BPHE190
CTYR118
site_idAC5
Number of Residues1
Detailsbinding site for residue MC3 D 700
ChainResidue
DPHE190
site_idAC6
Number of Residues8
Detailsbinding site for Di-peptide PHE C 103 and LYS C 110
ChainResidue
CTHR80
CLEU81
CSER102
CSER104
CPRO105
CGLY108
CLYS109
CASN111
Functional Information from PROSITE/UniProt
site_idPS00558
Number of Residues23
DetailsEUKARYOTIC_PORIN Eukaryotic mitochondrial porin signature. YqiDPdAcfsAKVNNssliGLgY
ChainResidueDetails
ATYR225-TYR247
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues656
DetailsTransmembrane: {"description":"Beta stranded","evidences":[{"source":"PubMed","id":"18755977","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18832158","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues16
DetailsMotif: {"description":"Mitochondrial localization signal","evidences":[{"source":"UniProtKB","id":"J5JPV3","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues40
DetailsMotif: {"description":"C-terminal beta-signal","evidences":[{"source":"UniProtKB","id":"J5JPV3","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues8
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"Q60932","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues24
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"18755977","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2K4T","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues4
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_FI7
Number of Residues4
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_FI8
Number of Residues4
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"Q9Z2L0","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues4
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"Q60932","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues4
DetailsModified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"Q60932","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI11
Number of Residues4
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"Q60932","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI12
Number of Residues4
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI13
Number of Residues4
DetailsModified residue: {"description":"N6-acetyllysine; alternate","evidences":[{"source":"UniProtKB","id":"Q60932","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI14
Number of Residues4
DetailsModified residue: {"description":"Phosphoserine; by NEK1","evidences":[{"source":"PubMed","id":"20230784","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI15
Number of Residues4
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI16
Number of Residues4
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"Q60932","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI17
Number of Residues4
DetailsModified residue: {"description":"N6-acetyllysine; alternate","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI18
Number of Residues4
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_FI19
Number of Residues16
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_FI20
Number of Residues4
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_FI21
Number of Residues8
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_FI22
Number of Residues4
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_FI23
Number of Residues4
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate","evidences":[{"source":"PubMed","id":"25621951","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

250359

PDB entries from 2026-03-11

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