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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

6TIQ

Refined solution NMR structure of hVDAC-1 in detergent micelles

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0001662biological_processbehavioral fear response
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
A0007268biological_processchemical synaptic transmission
A0007270biological_processneuron-neuron synaptic transmission
A0007612biological_processlearning
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
A0043065biological_processpositive regulation of apoptotic process
A0043066biological_processnegative regulation of apoptotic process
A0044325molecular_functiontransmembrane transporter binding
A0045121cellular_componentmembrane raft
A0045202cellular_componentsynapse
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
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
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 Residues164
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 Residues2
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"Q60932","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues6
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"18755977","evidenceCode":"ECO:0000269"}]}
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":"PubMed","id":"31015432","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18832158","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI5
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_FI6
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"Q9Z2L0","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"Q60932","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues1
DetailsModified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"Q60932","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues1
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"Q60932","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI11
Number of Residues1
DetailsModified residue: {"description":"N6-acetyllysine; alternate","evidences":[{"source":"UniProtKB","id":"Q60932","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI12
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine; by NEK1","evidences":[{"source":"PubMed","id":"20230784","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI13
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI14
Number of Residues1
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"Q60932","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI15
Number of Residues1
DetailsModified residue: {"description":"N6-acetyllysine; alternate","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI16
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_FI17
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_FI18
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_FI19
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_FI20
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_FI21
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

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PDB entries from 2025-08-27

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