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6CVN

Model of synthetic tau (R2x4) bound to the microtubule

Functional Information from GO Data
ChainGOidnamespacecontents
A0000226biological_processmicrotubule cytoskeleton organization
A0000278biological_processmitotic cell cycle
A0003924molecular_functionGTPase activity
A0005200molecular_functionstructural constituent of cytoskeleton
A0005515molecular_functionprotein binding
A0005525molecular_functionGTP binding
A0005737cellular_componentcytoplasm
A0005856cellular_componentcytoskeleton
A0005874cellular_componentmicrotubule
A0007017biological_processmicrotubule-based process
A0046872molecular_functionmetal ion binding
B0000226biological_processmicrotubule cytoskeleton organization
B0000278biological_processmitotic cell cycle
B0003924molecular_functionGTPase activity
B0005200molecular_functionstructural constituent of cytoskeleton
B0005525molecular_functionGTP binding
B0005737cellular_componentcytoplasm
B0005856cellular_componentcytoskeleton
B0005874cellular_componentmicrotubule
B0007017biological_processmicrotubule-based process
B0015630cellular_componentmicrotubule cytoskeleton
B0016787molecular_functionhydrolase activity
B0046872molecular_functionmetal ion binding
C0000226biological_processmicrotubule cytoskeleton organization
C0000278biological_processmitotic cell cycle
C0003924molecular_functionGTPase activity
C0005200molecular_functionstructural constituent of cytoskeleton
C0005515molecular_functionprotein binding
C0005525molecular_functionGTP binding
C0005737cellular_componentcytoplasm
C0005856cellular_componentcytoskeleton
C0005874cellular_componentmicrotubule
C0007017biological_processmicrotubule-based process
C0046872molecular_functionmetal ion binding
D0008017molecular_functionmicrotubule binding
D0015631molecular_functiontubulin binding
Functional Information from PDB Data
site_idAC1
Number of Residues13
Detailsbinding site for residue GDP A 501
ChainResidue
AGLN11
AASP179
AASN206
ATYR224
AASN228
ACYS12
AGLN15
AASN101
ASER140
AGLY143
AGLY144
ATHR145
AGLY146

site_idAC2
Number of Residues21
Detailsbinding site for residue GTP B 501
ChainResidue
ALYS254
BGLY10
BGLN11
BALA12
BGLN15
BALA99
BALA100
BASN101
BSER140
BGLY143
BGLY144
BTHR145
BGLY146
BILE171
BTHR179
BGLU183
BASN206
BTYR224
BLEU227
BASN228
BMG502

site_idAC3
Number of Residues1
Detailsbinding site for residue MG B 502
ChainResidue
BGTP501

site_idAC4
Number of Residues13
Detailsbinding site for residue GDP C 501
ChainResidue
CGLN11
CCYS12
CGLN15
CILE16
CASN101
CSER140
CGLY143
CGLY144
CTHR145
CGLY146
CASP179
CASN206
CASN228

Functional Information from PROSITE/UniProt
site_idPS00227
Number of Residues7
DetailsTUBULIN Tubulin subunits alpha, beta, and gamma signature. GGGTGSG
ChainResidueDetails
BGLY142-GLY148
AGLY142-GLY148

site_idPS00228
Number of Residues4
DetailsTUBULIN_B_AUTOREG Tubulin-beta mRNA autoregulation signal. MREI
ChainResidueDetails
AMET1-ILE4

site_idPS00229
Number of Residues13
DetailsTAU_MAP_1 Tau and MAP proteins tubulin-binding repeat signature. GSkdNikHvPGGG
ChainResidueDetails
DGLY261-GLY273
DGLY292-GLY304
DGLY323-GLY335
DGLY354-GLY366

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues20
DetailsSITE: Not glycated => ECO:0000269|PubMed:9326300
ChainResidueDetails
DLYS225
DLYS312
DVAL318
DCYS322
DPRO332
DASN341
DLEU344
DGLU371
DTHR376
DLYS384
DASP386
DLYS241
DPRO396
DASN255
DSER258
DHIS268
DVAL275
DCYS291
DASP295
DHIS299

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: Phosphotyrosine; by TTBK1 => ECO:0000269|PubMed:16923168
ChainResidueDetails
DTYR198
BGLU71
BSER140
BGLY144
BTHR145
BTHR179
BASN206
BASN228

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: Phosphoserine; by PDPK1 and TTBK1 => ECO:0000269|PubMed:16923168
ChainResidueDetails
DSER199
CSER40

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: Phosphoserine; by PDPK1 and TTBK1 => ECO:0000269|PubMed:15546861, ECO:0000269|PubMed:16923168, ECO:0000269|PubMed:19451179, ECO:0000269|PubMed:9614189
ChainResidueDetails
DSER200
CLYS60

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: Phosphoserine; by CK1, PDPK1 and TTBK1 => ECO:0000269|PubMed:14761950, ECO:0000269|PubMed:15546861, ECO:0000269|PubMed:16923168, ECO:0000269|PubMed:19451179, ECO:0000269|PubMed:21327254, ECO:0000269|PubMed:9614189, ECO:0007744|PubMed:18220336, ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569
ChainResidueDetails
DSER203
BSER232

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: Phosphothreonine; by CK1 and PDPK1 => ECO:0000269|PubMed:14761950, ECO:0000269|PubMed:15546861, ECO:0000269|PubMed:19451179
ChainResidueDetails
DTHR206
ATHR292
CTHR287
CTHR292

site_idSWS_FT_FI7
Number of Residues1
DetailsMOD_RES: Phosphothreonine; by BRSK1, BRSK2, DYRK2 and PDPK1 => ECO:0000269|PubMed:15546861, ECO:0000269|PubMed:18599021, ECO:0000269|PubMed:19451179, ECO:0000269|PubMed:21985311, ECO:0000269|PubMed:9614189
ChainResidueDetails
DTHR213
CARG320

site_idSWS_FT_FI8
Number of Residues1
DetailsMOD_RES: Phosphoserine; by PKA => ECO:0000269|PubMed:15546861, ECO:0000269|PubMed:16443603, ECO:0000269|PubMed:19451179, ECO:0000269|PubMed:9614189
ChainResidueDetails
DSER215
CGLU448

site_idSWS_FT_FI9
Number of Residues1
DetailsMOD_RES: Phosphothreonine; by PDPK1 => ECO:0000269|PubMed:16443603, ECO:0000269|PubMed:19451179
ChainResidueDetails
DTHR218
CLYS60

site_idSWS_FT_FI10
Number of Residues2
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P10637
ChainResidueDetails
DLYS226
DCYS291
CLYS326

site_idSWS_FT_FI11
Number of Residues1
DetailsMOD_RES: Phosphothreonine; by GSK3-beta and PDPK1 => ECO:0000269|PubMed:14690523, ECO:0000269|PubMed:15546861, ECO:0000269|PubMed:16443603, ECO:0007744|PubMed:23186163
ChainResidueDetails
DTHR232

site_idSWS_FT_FI12
Number of Residues1
DetailsMOD_RES: Phosphoserine; by PDPK1 => ECO:0000269|PubMed:15546861, ECO:0000269|PubMed:16443603, ECO:0000269|PubMed:9614189, ECO:0007744|PubMed:23186163
ChainResidueDetails
DSER236
BLYS370

site_idSWS_FT_FI13
Number of Residues1
DetailsMOD_RES: Phosphoserine; by PHK => ECO:0000269|PubMed:16443603, ECO:0000269|PubMed:8999860
ChainResidueDetails
DSER238

site_idSWS_FT_FI14
Number of Residues1
DetailsMOD_RES: N6-methyllysine; alternate => ECO:0000250|UniProtKB:P10637
ChainResidueDetails
DCYS260

site_idSWS_FT_FI15
Number of Residues1
DetailsMOD_RES: Phosphoserine; by MARK1, MARK2, MARK3, MARK4, BRSK1, BRSK2 and PHK => ECO:0000269|PubMed:15546861, ECO:0000269|PubMed:16443603, ECO:0000269|PubMed:19451179, ECO:0000269|PubMed:21985311, ECO:0000269|PubMed:23666762, ECO:0000269|PubMed:7706316, ECO:0000269|PubMed:8999860, ECO:0000269|PubMed:9614189
ChainResidueDetails
DLYS263

site_idSWS_FT_FI16
Number of Residues1
DetailsMOD_RES: Deamidated asparagine; in tau and PHF-tau; partial => ECO:0000269|PubMed:1512244
ChainResidueDetails
DLYS280

site_idSWS_FT_FI17
Number of Residues10
DetailsMOD_RES: N6-acetyllysine; alternate => ECO:0000250|UniProtKB:P10637
ChainResidueDetails
DLEU282
DASP386
DHIS299
DLYS312
DVAL318
DCYS322
DPRO332
DLEU344
DASN348
DILE370

site_idSWS_FT_FI18
Number of Residues2
DetailsMOD_RES: Phosphoserine; by PHK => ECO:0000269|PubMed:8999860
ChainResidueDetails
DASN286
DCYS353

site_idSWS_FT_FI19
Number of Residues3
DetailsMOD_RES: Phosphoserine => ECO:0000269|PubMed:7706316
ChainResidueDetails
DLYS294
DLYS325
DASP357

site_idSWS_FT_FI20
Number of Residues1
DetailsMOD_RES: Phosphoserine; by PHK => ECO:0000269|PubMed:7706316, ECO:0000269|PubMed:8999860
ChainResidueDetails
DVAL306

site_idSWS_FT_FI21
Number of Residues1
DetailsMOD_RES: Omega-N-methylarginine => ECO:0000250|UniProtKB:P10637
ChainResidueDetails
DGLN350

site_idSWS_FT_FI22
Number of Residues1
DetailsMOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P10637
ChainResidueDetails
DSER395

site_idSWS_FT_FI23
Number of Residues1
DetailsMOD_RES: Phosphoserine; by CK1 and PDPK1 => ECO:0000269|PubMed:14761950, ECO:0000269|PubMed:15546861, ECO:0000269|PubMed:16443603, ECO:0000269|PubMed:19451179, ECO:0000269|PubMed:21327254, ECO:0000269|PubMed:9614189, ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163
ChainResidueDetails
DVAL397

site_idSWS_FT_FI24
Number of Residues1
DetailsMOD_RES: Phosphoserine; alternate => ECO:0007744|PubMed:19690332
ChainResidueDetails

site_idSWS_FT_FI25
Number of Residues2
DetailsCARBOHYD: O-linked (GlcNAc) serine => ECO:0000269|PubMed:21327254
ChainResidueDetails
DSER209
DSER239

site_idSWS_FT_FI26
Number of Residues8
DetailsCARBOHYD: N-linked (Glc) (glycation) lysine; in PHF-tau; in vitro => ECO:0000269|PubMed:9326300
ChainResidueDetails
DLYS226
DLYS235
DCYS260
DLYS281
DLEU282
DASN348
DGLY354
DILE370

site_idSWS_FT_FI27
Number of Residues1
DetailsCARBOHYD: O-linked (GlcNAc) serine; alternate => ECO:0000269|PubMed:21327254
ChainResidueDetails

site_idSWS_FT_FI28
Number of Residues3
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); in PHF-tau => ECO:0000269|PubMed:16443603
ChainResidueDetails
DASN255
DLYS312
DGLY354

site_idSWS_FT_FI29
Number of Residues11
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate => ECO:0000250|UniProtKB:P10637
ChainResidueDetails
DILE370
DASP386
DCYS260
DLEU282
DHIS299
DVAL318
DCYS322
DPRO332
DLEU344
DASN348

site_idSWS_FT_FI30
Number of Residues2
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:P10637
ChainResidueDetails
DHIS268
DTHR376

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PDB entries from 2024-07-24

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