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

8G55

Temperature-dependent structures of tau aggregates

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
G0008017molecular_functionmicrotubule binding
G0015631molecular_functiontubulin binding
H0008017molecular_functionmicrotubule binding
H0015631molecular_functiontubulin binding
I0008017molecular_functionmicrotubule binding
I0015631molecular_functiontubulin binding
J0008017molecular_functionmicrotubule binding
J0015631molecular_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 Residues40
DetailsSITE: Not glycated => ECO:0000269|PubMed:9326300
ChainResidueDetails
AASN381
CGLU391
CILE392
CTYR394
DASN381
DGLU391
DILE392
DTYR394
EASN381
EGLU391
EILE392
AGLU391
ETYR394
FASN381
FGLU391
FILE392
FTYR394
GASN381
GGLU391
GILE392
GTYR394
HASN381
AILE392
HGLU391
HILE392
HTYR394
IASN381
IGLU391
IILE392
ITYR394
JASN381
JGLU391
JILE392
ATYR394
JTYR394
BASN381
BGLU391
BILE392
BTYR394
CASN381

site_idSWS_FT_FI2
Number of Residues10
DetailsMOD_RES: Phosphoserine; by SGK1 => ECO:0000269|PubMed:16982696
ChainResidueDetails
ASER214
JSER214
BSER214
CSER214
DSER214
ESER214
FSER214
GSER214
HSER214
ISER214

site_idSWS_FT_FI3
Number of Residues10
DetailsMOD_RES: Phosphoserine; in PHF-tau => ECO:0000269|PubMed:1899488
ChainResidueDetails
ASER396
JSER396
BSER396
CSER396
DSER396
ESER396
FSER396
GSER396
HSER396
ISER396

site_idSWS_FT_FI4
Number of Residues10
DetailsCARBOHYD: N-linked (Glc) (glycation) lysine; in PHF-tau; in vitro => ECO:0000269|PubMed:9326300
ChainResidueDetails
ALYS383
JLYS383
BLYS383
CLYS383
DLYS383
ELYS383
FLYS383
GLYS383
HLYS383
ILYS383

223790

PDB entries from 2024-08-14

PDB statisticsPDBj update infoContact PDBjnumon