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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

8VDO

Cryogenic electron microscopy model of full-length talin lacking F2, R12 and FABD.

Functional Information from GO Data
ChainGOidnamespacecontents
A0001726cellular_componentruffle
A0001786molecular_functionphosphatidylserine binding
A0003779molecular_functionactin binding
A0005178molecular_functionintegrin binding
A0005200molecular_functionstructural constituent of cytoskeleton
A0005515molecular_functionprotein binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0005856cellular_componentcytoskeleton
A0005886cellular_componentplasma membrane
A0005912cellular_componentadherens junction
A0005925cellular_componentfocal adhesion
A0006091biological_processgeneration of precursor metabolites and energy
A0007044biological_processcell-substrate junction assembly
A0007155biological_processcell adhesion
A0007229biological_processintegrin-mediated signaling pathway
A0008218biological_processbioluminescence
A0009986cellular_componentcell surface
A0017166molecular_functionvinculin binding
A0030036biological_processactin cytoskeleton organization
A0030274molecular_functionLIM domain binding
A0030866biological_processcortical actin cytoskeleton organization
A0032587cellular_componentruffle membrane
A0033622biological_processintegrin activation
A0034329biological_processcell junction assembly
A0034451cellular_componentcentriolar satellite
A0035091molecular_functionphosphatidylinositol binding
A0043622biological_processcortical microtubule organization
A0051015molecular_functionactin filament binding
A0070161cellular_componentanchoring junction
A0098609biological_processcell-cell adhesion
Functional Information from PROSITE/UniProt
site_idPS00660
Number of Residues29
DetailsFERM_1 FERM domain signature 1. WLdhgRtLreQg.Veehetll.Lrrk..FFysD
ChainResidueDetails
ATRP173-ASP201
site_idPS00661
Number of Residues30
DetailsFERM_2 FERM domain signature 2. HkncgqmseiEAkvrYVkl.ArsLktYGvSF
ChainResidueDetails
AHIS283-PHE312
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues130
DetailsRegion: {"description":"Helical bundle R2","evidences":[{"source":"PubMed","id":"23389036","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues124
DetailsRegion: {"description":"Helical bundle R3","evidences":[{"source":"PubMed","id":"23389036","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues131
DetailsRegion: {"description":"Helical bundle R4","evidences":[{"source":"PubMed","id":"23389036","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues160
DetailsRegion: {"description":"Helical bundle R5","evidences":[{"source":"PubMed","id":"23389036","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues150
DetailsRegion: {"description":"Helical bundle R6","evidences":[{"source":"PubMed","id":"23389036","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues621
DetailsRegion: {"description":"Interaction with SYNM","evidences":[{"source":"UniProtKB","id":"P54939","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues95
DetailsRegion: {"description":"Helical bundle R7A; Interaction with KANK1","evidences":[{"source":"PubMed","id":"27410476","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23389036","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues300
DetailsRegion: {"description":"Interaction with VCL and F-actin","evidences":[{"source":"PubMed","id":"20610383","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues119
DetailsRegion: {"description":"Helical bundle R8","evidences":[{"source":"PubMed","id":"23389036","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues72
DetailsRegion: {"description":"Helical bundle R7B; Interaction with KANK1","evidences":[{"source":"PubMed","id":"27410476","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23389036","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI11
Number of Residues167
DetailsRegion: {"description":"Helical bundle R9","evidences":[{"source":"PubMed","id":"23389036","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI12
Number of Residues150
DetailsRegion: {"description":"Helical bundle R10","evidences":[{"source":"PubMed","id":"23389036","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI13
Number of Residues5
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"21183079","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI14
Number of Residues5
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"Q9Y490","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI15
Number of Residues1
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"15592455","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"18034455","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI16
Number of Residues3
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"Q9Y490","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI17
Number of Residues1
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"23806337","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI18
Number of Residues2
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"Q9Y490","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

247536

PDB entries from 2026-01-14

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