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

7QKX

In vitro assembled 266/297 - 391 tau filaments with MgSO4 and NaCl (15b)

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
G0008017molecular_functionmicrotubule binding
G0015631molecular_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
AGLY261-GLY273
AGLY292-GLY304
AGLY323-GLY335
AGLY355-GLY367

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues42
DetailsSITE: Not glycated => ECO:0000269|PubMed:9326300
ChainResidueDetails
ALYS24
CLYS67
CASN381
CGLU391
CILE392
CTYR394
ELYS24
ELYS44
ELYS67
EASN381
EGLU391
ALYS44
EILE392
ETYR394
GLYS24
GLYS44
GLYS67
GASN381
GGLU391
GILE392
GTYR394
BLYS24
ALYS67
BLYS44
BLYS67
BASN381
BGLU391
BILE392
BTYR394
DLYS24
DLYS44
DLYS67
DASN381
AASN381
DGLU391
DILE392
DTYR394
AGLU391
AILE392
ATYR394
CLYS24
CLYS44

site_idSWS_FT_FI2
Number of Residues6
DetailsMOD_RES: N-acetylalanine => ECO:0000269|PubMed:1512244
ChainResidueDetails
AALA2
CALA2
EALA2
GALA2
BALA2
DALA2

site_idSWS_FT_FI3
Number of Residues6
DetailsMOD_RES: Phosphotyrosine; by FYN => ECO:0000269|PubMed:14999081
ChainResidueDetails
ATYR18
CTYR18
ETYR18
GTYR18
BTYR18
DTYR18

site_idSWS_FT_FI4
Number of Residues6
DetailsMOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P10637
ChainResidueDetails
ATYR29
CTYR29
ETYR29
GTYR29
BTYR29
DTYR29

site_idSWS_FT_FI5
Number of Residues12
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P19332
ChainResidueDetails
ASER46
BSER61
DSER46
DSER61
ASER61
CSER46
CSER61
ESER46
ESER61
GSER46
GSER61
BSER46

site_idSWS_FT_FI6
Number of Residues12
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P10637
ChainResidueDetails
ATHR69
BTHR111
DTHR69
DTHR111
ATHR111
CTHR69
CTHR111
ETHR69
ETHR111
GTHR69
GTHR111
BTHR69

site_idSWS_FT_FI7
Number of Residues6
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P19332
ChainResidueDetails
ATHR71
CTHR71
ETHR71
GTHR71
BTHR71
DTHR71

site_idSWS_FT_FI8
Number of Residues6
DetailsMOD_RES: Phosphoserine; by SGK1 => ECO:0000269|PubMed:16982696
ChainResidueDetails
ASER214
CSER214
ESER214
GSER214
BSER214
DSER214

site_idSWS_FT_FI9
Number of Residues6
DetailsMOD_RES: Phosphoserine; in PHF-tau => ECO:0000269|PubMed:1899488
ChainResidueDetails
ASER396
CSER396
ESER396
GSER396
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
ALYS87
BLYS383
DLYS87
DLYS383
ALYS383
CLYS87
CLYS383
ELYS87
ELYS383
GLYS87
GLYS383
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
ALYS44
DLYS44
CLYS44
ELYS44
GLYS44
BLYS44

223532

PDB entries from 2024-08-07

PDB statisticsPDBj update infoContact PDBjnumon