4GLR
Structure of the anti-ptau Fab (pT231/pS235_1) in complex with phosphoepitope pT231/pS235
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE PO4 H 301 |
Chain | Residue |
H | PRO123 |
H | LYS214 |
H | SER215 |
H | HOH588 |
H | HOH594 |
I | SER121 |
I | SER122 |
I | GLU123 |
I | HOH435 |
site_id | AC2 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE PO4 K 301 |
Chain | Residue |
J | ALA125 |
J | LYS214 |
K | SER121 |
K | SER122 |
K | GLU123 |
K | HOH421 |
K | HOH509 |
Functional Information from PROSITE/UniProt
site_id | PS00290 |
Number of Residues | 7 |
Details | IG_MHC Immunoglobulins and major histocompatibility complex proteins signature. YSCQVTH |
Chain | Residue | Details |
I | TYR191-HIS197 | |
H | TYR194-HIS200 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 4 |
Details | SITE: Not glycated => ECO:0000269|PubMed:9326300 |
Chain | Residue | Details |
A | LYS224 | |
A | LYS240 | |
B | LYS224 | |
B | LYS240 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P10637 |
Chain | Residue | Details |
A | LYS225 | |
B | LYS225 |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | MOD_RES: Phosphothreonine; by GSK3-beta and PDPK1 => ECO:0000269|PubMed:14690523, ECO:0000269|PubMed:15546861, ECO:0000269|PubMed:16443603, ECO:0007744|PubMed:23186163 |
Chain | Residue | Details |
A | TPO231 | |
B | TPO231 |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine; by PDPK1 => ECO:0000269|PubMed:15546861, ECO:0000269|PubMed:16443603, ECO:0000269|PubMed:9614189, ECO:0007744|PubMed:23186163 |
Chain | Residue | Details |
A | SEP235 | |
B | SEP235 |
site_id | SWS_FT_FI5 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine; by PHK => ECO:0000269|PubMed:16443603, ECO:0000269|PubMed:8999860 |
Chain | Residue | Details |
A | SER237 | |
B | SER237 |
site_id | SWS_FT_FI6 |
Number of Residues | 4 |
Details | CARBOHYD: N-linked (Glc) (glycation) lysine; in PHF-tau; in vitro => ECO:0000269|PubMed:9326300 |
Chain | Residue | Details |
A | LYS225 | |
A | LYS234 | |
B | LYS225 | |
B | LYS234 |
site_id | SWS_FT_FI7 |
Number of Residues | 2 |
Details | CARBOHYD: O-linked (GlcNAc) serine => ECO:0000269|PubMed:21327254 |
Chain | Residue | Details |
A | SER238 | |
B | SER238 |