7LC9
Cryo-EM structure of the N-terminal alpha-synuclein truncation 41-140
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0014059 | biological_process | regulation of dopamine secretion |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0014059 | biological_process | regulation of dopamine secretion |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0014059 | biological_process | regulation of dopamine secretion |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0014059 | biological_process | regulation of dopamine secretion |
| E | 0005737 | cellular_component | cytoplasm |
| E | 0014059 | biological_process | regulation of dopamine secretion |
| F | 0005737 | cellular_component | cytoplasm |
| F | 0014059 | biological_process | regulation of dopamine secretion |
| G | 0005737 | cellular_component | cytoplasm |
| G | 0014059 | biological_process | regulation of dopamine secretion |
| H | 0005737 | cellular_component | cytoplasm |
| H | 0014059 | biological_process | regulation of dopamine secretion |
| I | 0005737 | cellular_component | cytoplasm |
| I | 0014059 | biological_process | regulation of dopamine secretion |
| J | 0005737 | cellular_component | cytoplasm |
| J | 0014059 | biological_process | regulation of dopamine secretion |
| K | 0005737 | cellular_component | cytoplasm |
| K | 0014059 | biological_process | regulation of dopamine secretion |
| L | 0005737 | cellular_component | cytoplasm |
| L | 0014059 | biological_process | regulation of dopamine secretion |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 12 |
| Details | BINDING: BINDING => ECO:0000305 |
| Chain | Residue | Details |
| F | HIS50 | |
| E | HIS50 | |
| L | HIS50 | |
| G | HIS50 | |
| A | HIS50 | |
| H | HIS50 | |
| B | HIS50 | |
| I | HIS50 | |
| C | HIS50 | |
| J | HIS50 | |
| D | HIS50 | |
| K | HIS50 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 12 |
| Details | MOD_RES: Phosphoserine => ECO:0000269|PubMed:10617630 |
| Chain | Residue | Details |
| F | SER87 | |
| E | SER87 | |
| L | SER87 | |
| G | SER87 | |
| A | SER87 | |
| H | SER87 | |
| B | SER87 | |
| I | SER87 | |
| C | SER87 | |
| J | SER87 | |
| D | SER87 | |
| K | SER87 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 12 |
| Details | MOD_RES: Phosphotyrosine; by FYN => ECO:0000269|PubMed:11162638, ECO:0000269|PubMed:12893833 |
| Chain | Residue | Details |
| F | TYR125 | |
| E | TYR125 | |
| L | TYR125 | |
| G | TYR125 | |
| A | TYR125 | |
| H | TYR125 | |
| B | TYR125 | |
| I | TYR125 | |
| C | TYR125 | |
| J | TYR125 | |
| D | TYR125 | |
| K | TYR125 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 12 |
| Details | MOD_RES: Phosphoserine; by BARK1, PLK2, CK2, CK1 and GRK5 => ECO:0000269|PubMed:10617630, ECO:0000269|PubMed:11813001, ECO:0000269|PubMed:24936070 |
| Chain | Residue | Details |
| F | SER129 | |
| E | SER129 | |
| L | SER129 | |
| G | SER129 | |
| A | SER129 | |
| H | SER129 | |
| B | SER129 | |
| I | SER129 | |
| C | SER129 | |
| J | SER129 | |
| D | SER129 | |
| K | SER129 |
