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4GLR

Structure of the anti-ptau Fab (pT231/pS235_1) in complex with phosphoepitope pT231/pS235

Functional Information from PDB Data
site_idAC1
Number of Residues9
DetailsBINDING SITE FOR RESIDUE PO4 H 301
ChainResidue
HPRO123
HLYS214
HSER215
HHOH588
HHOH594
ISER121
ISER122
IGLU123
IHOH435

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE PO4 K 301
ChainResidue
JALA125
JLYS214
KSER121
KSER122
KGLU123
KHOH421
KHOH509

Functional Information from PROSITE/UniProt
site_idPS00290
Number of Residues7
DetailsIG_MHC Immunoglobulins and major histocompatibility complex proteins signature. YSCQVTH
ChainResidueDetails
ITYR191-HIS197
HTYR194-HIS200

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsSITE: Not glycated => ECO:0000269|PubMed:9326300
ChainResidueDetails
ALYS224
ALYS240
BLYS224
BLYS240

site_idSWS_FT_FI2
Number of Residues2
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P10637
ChainResidueDetails
ALYS225
BLYS225

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: Phosphothreonine; by GSK3-beta and PDPK1 => ECO:0000269|PubMed:14690523, ECO:0000269|PubMed:15546861, ECO:0000269|PubMed:16443603, ECO:0007744|PubMed:23186163
ChainResidueDetails
ATPO231
BTPO231

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: Phosphoserine; by PDPK1 => ECO:0000269|PubMed:15546861, ECO:0000269|PubMed:16443603, ECO:0000269|PubMed:9614189, ECO:0007744|PubMed:23186163
ChainResidueDetails
ASEP235
BSEP235

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: Phosphoserine; by PHK => ECO:0000269|PubMed:16443603, ECO:0000269|PubMed:8999860
ChainResidueDetails
ASER237
BSER237

site_idSWS_FT_FI6
Number of Residues4
DetailsCARBOHYD: N-linked (Glc) (glycation) lysine; in PHF-tau; in vitro => ECO:0000269|PubMed:9326300
ChainResidueDetails
ALYS225
ALYS234
BLYS225
BLYS234

site_idSWS_FT_FI7
Number of Residues2
DetailsCARBOHYD: O-linked (GlcNAc) serine => ECO:0000269|PubMed:21327254
ChainResidueDetails
ASER238
BSER238

222926

PDB entries from 2024-07-24

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