8OHI
Structure of the Fmoc-Tau-PAM4 Type 2 amyloid fibril
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0015631 | molecular_function | tubulin binding |
| B | 0015631 | molecular_function | tubulin binding |
| C | 0015631 | molecular_function | tubulin binding |
| D | 0015631 | molecular_function | tubulin binding |
| E | 0015631 | molecular_function | tubulin binding |
| F | 0015631 | molecular_function | tubulin binding |
| G | 0015631 | molecular_function | tubulin binding |
| H | 0015631 | molecular_function | tubulin binding |
| I | 0015631 | molecular_function | tubulin binding |
| J | 0015631 | molecular_function | tubulin binding |
| K | 0015631 | molecular_function | tubulin binding |
| L | 0015631 | molecular_function | tubulin binding |
| M | 0015631 | molecular_function | tubulin binding |
| N | 0015631 | molecular_function | tubulin binding |
| O | 0015631 | molecular_function | tubulin binding |
| P | 0015631 | molecular_function | tubulin binding |
| Q | 0015631 | molecular_function | tubulin binding |
| R | 0015631 | molecular_function | tubulin binding |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 18 |
| Details | MOD_RES: Phosphoserine; by PHK => ECO:0000269|PubMed:8999860 |
| Chain | Residue | Details |
| A | SER352 | |
| J | SER352 | |
| K | SER352 | |
| L | SER352 | |
| M | SER352 | |
| N | SER352 | |
| O | SER352 | |
| P | SER352 | |
| Q | SER352 | |
| R | SER352 | |
| B | SER352 | |
| C | SER352 | |
| D | SER352 | |
| E | SER352 | |
| F | SER352 | |
| G | SER352 | |
| H | SER352 | |
| I | SER352 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 18 |
| Details | MOD_RES: Phosphoserine => ECO:0000269|PubMed:7706316 |
| Chain | Residue | Details |
| A | SER356 | |
| J | SER356 | |
| K | SER356 | |
| L | SER356 | |
| M | SER356 | |
| N | SER356 | |
| O | SER356 | |
| P | SER356 | |
| Q | SER356 | |
| R | SER356 | |
| B | SER356 | |
| C | SER356 | |
| D | SER356 | |
| E | SER356 | |
| F | SER356 | |
| G | SER356 | |
| H | SER356 | |
| I | SER356 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 18 |
| Details | CARBOHYD: N-linked (Glc) (glycation) lysine; in PHF-tau; in vitro => ECO:0000269|PubMed:9326300 |
| Chain | Residue | Details |
| A | LYS353 | |
| J | LYS353 | |
| K | LYS353 | |
| L | LYS353 | |
| M | LYS353 | |
| N | LYS353 | |
| O | LYS353 | |
| P | LYS353 | |
| Q | LYS353 | |
| R | LYS353 | |
| B | LYS353 | |
| C | LYS353 | |
| D | LYS353 | |
| E | LYS353 | |
| F | LYS353 | |
| G | LYS353 | |
| H | LYS353 | |
| I | LYS353 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 36 |
| Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); in PHF-tau => ECO:0000269|PubMed:16443603 |
| Chain | Residue | Details |
| A | LYS353 | |
| F | LYS353 | |
| G | LYS353 | |
| H | LYS353 | |
| I | LYS353 | |
| J | LYS353 | |
| K | LYS353 | |
| L | LYS353 | |
| M | LYS353 | |
| N | LYS353 | |
| O | LYS353 | |
| B | LYS353 | |
| P | LYS353 | |
| Q | LYS353 | |
| R | LYS353 | |
| C | LYS353 | |
| D | LYS353 | |
| E | LYS353 |
