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7QK5

In vitro assembled 266/297 - 391 tau filaments with KCl (10a)

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
K0008017molecular_functionmicrotubule binding
K0015631molecular_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 Residues63
DetailsSITE: Not glycated => ECO:0000269|PubMed:9326300
ChainResidueDetails
ALYS24
KLYS67
KASN381
KGLU391
KILE392
KTYR394
BLYS24
BLYS44
BLYS67
BASN381
BGLU391
ALYS44
BILE392
BTYR394
CLYS24
CLYS44
CLYS67
CASN381
CGLU391
CILE392
CTYR394
DLYS24
ALYS67
DLYS44
DLYS67
DASN381
DGLU391
DILE392
DTYR394
ELYS24
ELYS44
ELYS67
EASN381
AASN381
EGLU391
EILE392
ETYR394
FLYS24
FLYS44
FLYS67
FASN381
FGLU391
FILE392
FTYR394
AGLU391
GLYS24
GLYS44
GLYS67
GASN381
GGLU391
GILE392
GTYR394
HLYS24
HLYS44
HLYS67
AILE392
HASN381
HGLU391
HILE392
HTYR394
ATYR394
KLYS24
KLYS44

site_idSWS_FT_FI2
Number of Residues9
DetailsMOD_RES: N-acetylalanine => ECO:0000269|PubMed:1512244
ChainResidueDetails
AALA2
KALA2
BALA2
CALA2
DALA2
EALA2
FALA2
GALA2
HALA2

site_idSWS_FT_FI3
Number of Residues9
DetailsMOD_RES: Phosphotyrosine; by FYN => ECO:0000269|PubMed:14999081
ChainResidueDetails
ATYR18
KTYR18
BTYR18
CTYR18
DTYR18
ETYR18
FTYR18
GTYR18
HTYR18

site_idSWS_FT_FI4
Number of Residues9
DetailsMOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P10637
ChainResidueDetails
ATYR29
KTYR29
BTYR29
CTYR29
DTYR29
ETYR29
FTYR29
GTYR29
HTYR29

site_idSWS_FT_FI5
Number of Residues18
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P19332
ChainResidueDetails
ASER46
DSER61
ESER46
ESER61
FSER46
FSER61
GSER46
GSER61
HSER46
HSER61
ASER61
KSER46
KSER61
BSER46
BSER61
CSER46
CSER61
DSER46

site_idSWS_FT_FI6
Number of Residues18
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P10637
ChainResidueDetails
ATHR69
DTHR111
ETHR69
ETHR111
FTHR69
FTHR111
GTHR69
GTHR111
HTHR69
HTHR111
ATHR111
KTHR69
KTHR111
BTHR69
BTHR111
CTHR69
CTHR111
DTHR69

site_idSWS_FT_FI7
Number of Residues9
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P19332
ChainResidueDetails
ATHR71
KTHR71
BTHR71
CTHR71
DTHR71
ETHR71
FTHR71
GTHR71
HTHR71

site_idSWS_FT_FI8
Number of Residues9
DetailsMOD_RES: Phosphoserine; by SGK1 => ECO:0000269|PubMed:16982696
ChainResidueDetails
ASER214
KSER214
BSER214
CSER214
DSER214
ESER214
FSER214
GSER214
HSER214

site_idSWS_FT_FI9
Number of Residues9
DetailsMOD_RES: Phosphoserine; in PHF-tau => ECO:0000269|PubMed:1899488
ChainResidueDetails
ASER396
KSER396
BSER396
CSER396
DSER396
ESER396
FSER396
GSER396
HSER396

site_idSWS_FT_FI10
Number of Residues18
DetailsCARBOHYD: N-linked (Glc) (glycation) lysine; in PHF-tau; in vitro => ECO:0000269|PubMed:9326300
ChainResidueDetails
ALYS87
DLYS383
ELYS87
ELYS383
FLYS87
FLYS383
GLYS87
GLYS383
HLYS87
HLYS383
ALYS383
KLYS87
KLYS383
BLYS87
BLYS383
CLYS87
CLYS383
DLYS87

site_idSWS_FT_FI11
Number of Residues18
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:P10637
ChainResidueDetails
ALYS44
ELYS44
FLYS44
GLYS44
HLYS44
KLYS44
BLYS44
CLYS44
DLYS44

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PDB entries from 2024-07-31

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