Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

7QK1

In vitro assembled 297-394 tau filaments in PBS (35d)

Functional Information from GO Data
ChainGOidnamespacecontents
A0008017molecular_functionmicrotubule binding
A0015631molecular_functiontubulin binding
B0008017molecular_functionmicrotubule binding
B0015631molecular_functiontubulin binding
C0008017molecular_functionmicrotubule binding
C0015631molecular_functiontubulin binding
D0008017molecular_functionmicrotubule binding
D0015631molecular_functiontubulin binding
E0008017molecular_functionmicrotubule binding
E0015631molecular_functiontubulin binding
F0008017molecular_functionmicrotubule binding
F0015631molecular_functiontubulin binding
Functional Information from PROSITE/UniProt
site_idPS00229
Number of Residues13
DetailsTAU_MAP_1 Tau and MAP proteins tubulin-binding repeat signature. GSteNlkHqPGGG
ChainResidueDetails
CGLY261-GLY273
CGLY292-GLY304
CGLY323-GLY335
CGLY355-GLY367

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues42
DetailsSITE: Not glycated => ECO:0000269|PubMed:9326300
ChainResidueDetails
CLYS24
ELYS67
EASN381
EGLU391
EILE392
ETYR394
FLYS24
FLYS44
FLYS67
FASN381
FGLU391
CLYS44
FILE392
FTYR394
ALYS24
ALYS44
ALYS67
AASN381
AGLU391
AILE392
ATYR394
BLYS24
CLYS67
BLYS44
BLYS67
BASN381
BGLU391
BILE392
BTYR394
DLYS24
DLYS44
DLYS67
DASN381
CASN381
DGLU391
DILE392
DTYR394
CGLU391
CILE392
CTYR394
ELYS24
ELYS44

site_idSWS_FT_FI2
Number of Residues6
DetailsMOD_RES: N-acetylalanine => ECO:0000269|PubMed:1512244
ChainResidueDetails
CALA2
EALA2
FALA2
AALA2
BALA2
DALA2

site_idSWS_FT_FI3
Number of Residues6
DetailsMOD_RES: Phosphotyrosine; by FYN => ECO:0000269|PubMed:14999081
ChainResidueDetails
CTYR18
ETYR18
FTYR18
ATYR18
BTYR18
DTYR18

site_idSWS_FT_FI4
Number of Residues6
DetailsMOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P10637
ChainResidueDetails
CTYR29
ETYR29
FTYR29
ATYR29
BTYR29
DTYR29

site_idSWS_FT_FI5
Number of Residues12
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P19332
ChainResidueDetails
CSER46
BSER61
DSER46
DSER61
CSER61
ESER46
ESER61
FSER46
FSER61
ASER46
ASER61
BSER46

site_idSWS_FT_FI6
Number of Residues12
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P10637
ChainResidueDetails
CTHR69
BTHR111
DTHR69
DTHR111
CTHR111
ETHR69
ETHR111
FTHR69
FTHR111
ATHR69
ATHR111
BTHR69

site_idSWS_FT_FI7
Number of Residues6
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P19332
ChainResidueDetails
CTHR71
ETHR71
FTHR71
ATHR71
BTHR71
DTHR71

site_idSWS_FT_FI8
Number of Residues6
DetailsMOD_RES: Phosphoserine; by SGK1 => ECO:0000269|PubMed:16982696
ChainResidueDetails
CSER214
ESER214
FSER214
ASER214
BSER214
DSER214

site_idSWS_FT_FI9
Number of Residues6
DetailsMOD_RES: Phosphoserine; in PHF-tau => ECO:0000269|PubMed:1899488
ChainResidueDetails
CSER396
ESER396
FSER396
ASER396
BSER396
DSER396

site_idSWS_FT_FI10
Number of Residues12
DetailsCARBOHYD: N-linked (Glc) (glycation) lysine; in PHF-tau; in vitro => ECO:0000269|PubMed:9326300
ChainResidueDetails
CLYS87
BLYS383
DLYS87
DLYS383
CLYS383
ELYS87
ELYS383
FLYS87
FLYS383
ALYS87
ALYS383
BLYS87

site_idSWS_FT_FI11
Number of Residues12
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:P10637
ChainResidueDetails
CLYS44
DLYS44
ELYS44
FLYS44
ALYS44
BLYS44

223166

PDB entries from 2024-07-31

PDB statisticsPDBj update infoContact PDBjnumon