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8VDR

Cryogenic electron microscopy model of full-length talin without R12 and FABD

Functional Information from GO Data
ChainGOidnamespacecontents
A0001726cellular_componentruffle
A0001786molecular_functionphosphatidylserine binding
A0005178molecular_functionintegrin binding
A0005515molecular_functionprotein binding
A0005737cellular_componentcytoplasm
A0005856cellular_componentcytoskeleton
A0005886cellular_componentplasma membrane
A0005912cellular_componentadherens junction
A0005925cellular_componentfocal adhesion
A0007044biological_processcell-substrate junction assembly
A0007229biological_processintegrin-mediated signaling pathway
A0009986cellular_componentcell surface
A0017166molecular_functionvinculin binding
A0030274molecular_functionLIM domain binding
A0030866biological_processcortical actin cytoskeleton organization
A0032587cellular_componentruffle membrane
A0033622biological_processintegrin activation
A0035091molecular_functionphosphatidylinositol binding
A0042995cellular_componentcell projection
A0043622biological_processcortical microtubule organization
A0070161cellular_componentanchoring junction
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 Residues4
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:Q9Y490
ChainResidueDetails
ATHR167
ATHR1142
ATHR1263
ATHR1855

site_idSWS_FT_FI2
Number of Residues6
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q9Y490
ChainResidueDetails
ASER405
ASER1021
ASER1201
ASER1225
ASER1323
ASER1849

site_idSWS_FT_FI3
Number of Residues7
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:21183079
ChainResidueDetails
ASER425
ASER446
ASER620
ASER729
ASER1328
ASER1878
ASER2040

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: Phosphotyrosine => ECO:0007744|PubMed:15592455, ECO:0007744|PubMed:18034455
ChainResidueDetails
ATYR1116

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: N6-acetyllysine => ECO:0007744|PubMed:23806337
ChainResidueDetails
ALYS1544

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:Q9Y490
ChainResidueDetails
ALYS2031
ALYS2115

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PDB entries from 2024-11-06

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