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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

7TCV

VDAC K12E mutant

This is a non-PDB format compatible entry.
Functional Information from GO Data
ChainGOidnamespacecontents
XXX0000166molecular_functionnucleotide binding
XXX0001662biological_processbehavioral fear response
XXX0005244molecular_functionvoltage-gated monoatomic ion channel activity
XXX0005253molecular_functionmonoatomic anion channel activity
XXX0005515molecular_functionprotein binding
XXX0005524molecular_functionATP binding
XXX0005739cellular_componentmitochondrion
XXX0005741cellular_componentmitochondrial outer membrane
XXX0005743cellular_componentmitochondrial inner membrane
XXX0005757cellular_componentmitochondrial permeability transition pore complex
XXX0005886cellular_componentplasma membrane
XXX0006086biological_processpyruvate decarboxylation to acetyl-CoA
XXX0006811biological_processmonoatomic ion transport
XXX0006820biological_processmonoatomic anion transport
XXX0006851biological_processmitochondrial calcium ion transmembrane transport
XXX0006869biological_processlipid transport
XXX0006915biological_processapoptotic process
XXX0007268biological_processchemical synaptic transmission
XXX0007270biological_processneuron-neuron synaptic transmission
XXX0007612biological_processlearning
XXX0008021cellular_componentsynaptic vesicle
XXX0008142molecular_functionoxysterol binding
XXX0008289molecular_functionlipid binding
XXX0008308molecular_functionvoltage-gated monoatomic anion channel activity
XXX0015288molecular_functionporin activity
XXX0015485molecular_functioncholesterol binding
XXX0016020cellular_componentmembrane
XXX0019901molecular_functionprotein kinase binding
XXX0022832molecular_functionvoltage-gated channel activity
XXX0030855biological_processepithelial cell differentiation
XXX0031210molecular_functionphosphatidylcholine binding
XXX0031966cellular_componentmitochondrial membrane
XXX0032991cellular_componentprotein-containing complex
XXX0036444biological_processcalcium import into the mitochondrion
XXX0042645cellular_componentmitochondrial nucleoid
XXX0042802molecular_functionidentical protein binding
XXX0043065biological_processpositive regulation of apoptotic process
XXX0043066biological_processnegative regulation of apoptotic process
XXX0043209cellular_componentmyelin sheath
XXX0044325molecular_functiontransmembrane transporter binding
XXX0044877molecular_functionprotein-containing complex binding
XXX0045121cellular_componentmembrane raft
XXX0046930cellular_componentpore complex
XXX0048787cellular_componentpresynaptic active zone membrane
XXX0055085biological_processtransmembrane transport
XXX0097001molecular_functionceramide binding
XXX0098656biological_processmonoatomic anion transmembrane transport
XXX0098839cellular_componentpostsynaptic density membrane
XXX0110099biological_processnegative regulation of calcium import into the mitochondrion
XXX1901524biological_processregulation of mitophagy
XXX1901526biological_processpositive regulation of mitophagy
XXX1905091biological_processpositive regulation of type 2 mitophagy
XXX1990542biological_processmitochondrial transmembrane transport
XXX2000378biological_processnegative regulation of reactive oxygen species metabolic process
Functional Information from PROSITE/UniProt
site_idPS00558
Number of Residues23
DetailsEUKARYOTIC_PORIN Eukaryotic mitochondrial porin signature. YqvDPdAcfsAKVNNssliGLgY
ChainResidueDetails
XXXTYR225-TYR247
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues163
DetailsTransmembrane: {"description":"Beta stranded","evidences":[{"source":"PubMed","id":"18988731","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"24908397","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4C69","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues6
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P21796","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues1
DetailsSite: {"description":"Involved in ceramide and phosphatidylcholine binding. Critical for channel structural stability and gating","evidences":[{"source":"UniProtKB","id":"P21796","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"Q9Z2L0","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"21183079","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues1
DetailsModified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"PubMed","id":"23806337","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues1
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"18034455","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"P21796","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues1
DetailsModified residue: {"description":"N6-acetyllysine; alternate","evidences":[{"source":"PubMed","id":"23576753","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI11
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine; by NEK1","evidences":[{"source":"UniProtKB","id":"P21796","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI12
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"21183079","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI13
Number of Residues1
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"23576753","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI14
Number of Residues1
DetailsModified residue: {"description":"N6-acetyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P21796","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI15
Number of Residues5
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_FI16
Number of Residues2
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_FI17
Number of Residues1
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"source":"UniProtKB","id":"P21796","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI18
Number of Residues1
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate","evidences":[{"source":"UniProtKB","id":"P21796","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

246031

PDB entries from 2025-12-10

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