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

8BGS

Tau Paired Helical Filament from Extracellular Vesicles from Alzheimer's disease brain

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
r0008017molecular_functionmicrotubule binding
r0015631molecular_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
rGLY261-GLY273
rGLY292-GLY304
rGLY323-GLY335
rGLY355-GLY367

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues49
DetailsSITE: Not glycated => ECO:0000269|PubMed:9326300
ChainResidueDetails
rLYS24
ALYS67
AASN381
AGLU391
AILE392
ATYR394
BLYS24
BLYS44
BLYS67
BASN381
BGLU391
rLYS44
BILE392
BTYR394
CLYS24
CLYS44
CLYS67
CASN381
CGLU391
CILE392
CTYR394
DLYS24
rLYS67
DLYS44
DLYS67
DASN381
DGLU391
DILE392
DTYR394
ELYS24
ELYS44
ELYS67
EASN381
rASN381
EGLU391
EILE392
ETYR394
FLYS24
FLYS44
FLYS67
FASN381
FGLU391
FILE392
FTYR394
rGLU391
rILE392
rTYR394
ALYS24
ALYS44

site_idSWS_FT_FI2
Number of Residues7
DetailsMOD_RES: N-acetylalanine => ECO:0000269|PubMed:1512244
ChainResidueDetails
rALA2
AALA2
BALA2
CALA2
DALA2
EALA2
FALA2

site_idSWS_FT_FI3
Number of Residues7
DetailsMOD_RES: Phosphotyrosine; by FYN => ECO:0000269|PubMed:14999081
ChainResidueDetails
rTYR18
ATYR18
BTYR18
CTYR18
DTYR18
ETYR18
FTYR18

site_idSWS_FT_FI4
Number of Residues7
DetailsMOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P10637
ChainResidueDetails
rTYR29
ATYR29
BTYR29
CTYR29
DTYR29
ETYR29
FTYR29

site_idSWS_FT_FI5
Number of Residues14
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P19332
ChainResidueDetails
rSER46
DSER61
ESER46
ESER61
FSER46
FSER61
rSER61
ASER46
ASER61
BSER46
BSER61
CSER46
CSER61
DSER46

site_idSWS_FT_FI6
Number of Residues14
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P10637
ChainResidueDetails
rTHR69
DTHR111
ETHR69
ETHR111
FTHR69
FTHR111
rTHR111
ATHR69
ATHR111
BTHR69
BTHR111
CTHR69
CTHR111
DTHR69

site_idSWS_FT_FI7
Number of Residues7
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P19332
ChainResidueDetails
rTHR71
ATHR71
BTHR71
CTHR71
DTHR71
ETHR71
FTHR71

site_idSWS_FT_FI8
Number of Residues7
DetailsMOD_RES: Phosphoserine; by SGK1 => ECO:0000269|PubMed:16982696
ChainResidueDetails
rSER214
ASER214
BSER214
CSER214
DSER214
ESER214
FSER214

site_idSWS_FT_FI9
Number of Residues7
DetailsMOD_RES: Phosphoserine; in PHF-tau => ECO:0000269|PubMed:1899488
ChainResidueDetails
rSER396
ASER396
BSER396
CSER396
DSER396
ESER396
FSER396

site_idSWS_FT_FI10
Number of Residues14
DetailsCARBOHYD: N-linked (Glc) (glycation) lysine; in PHF-tau; in vitro => ECO:0000269|PubMed:9326300
ChainResidueDetails
rLYS87
DLYS383
ELYS87
ELYS383
FLYS87
FLYS383
rLYS383
ALYS87
ALYS383
BLYS87
BLYS383
CLYS87
CLYS383
DLYS87

site_idSWS_FT_FI11
Number of Residues14
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:P10637
ChainResidueDetails
rLYS44
ELYS44
FLYS44
ALYS44
BLYS44
CLYS44
DLYS44

223532

PDB entries from 2024-08-07

PDB statisticsPDBj update infoContact PDBjnumon