9MOI
Structure of native murine cardiac thin filament at pCa=5.8 in Ca2+-free rotated state (lower strand)
Functional Information from PROSITE/UniProt
| site_id | PS00018 |
| Number of Residues | 13 |
| Details | EF_HAND_1 EF-hand calcium-binding domain. DEDGSGTVDfdEF |
| Chain | Residue | Details |
| G | ASP65-PHE77 | |
| G | ASP105-LEU117 | |
| G | ASP141-PHE153 |
| site_id | PS00326 |
| Number of Residues | 9 |
| Details | TROPOMYOSIN Tropomyosins signature. LKEAEtRAE |
| Chain | Residue | Details |
| K | LEU232-GLU240 |
| site_id | PS00406 |
| Number of Residues | 11 |
| Details | ACTINS_1 Actins signature 1. YVGDEAQs.KRG |
| Chain | Residue | Details |
| A | TYR53-GLY63 |
| site_id | PS00432 |
| Number of Residues | 9 |
| Details | ACTINS_2 Actins signature 2. WISKqEYDE |
| Chain | Residue | Details |
| A | TRP356-GLU364 |
| site_id | PS01132 |
| Number of Residues | 13 |
| Details | ACTINS_ACT_LIKE Actins and actin-related proteins signature. LLTEApLNPkaNR |
| Chain | Residue | Details |
| A | LEU104-ARG116 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | MOD_RES: N-acetylmethionine => ECO:0000250|UniProtKB:P09493 |
| Chain | Residue | Details |
| K | MET1 | |
| G | GLU116 | |
| G | ASP141 | |
| G | ASN143 | |
| G | ASP145 | |
| G | ARG147 | |
| G | GLU152 | |
| L | MET1 | |
| M | MET1 | |
| N | MET1 | |
| G | GLU76 | |
| G | ASP105 | |
| G | ASN107 | |
| G | ASP109 | |
| G | TYR111 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P04692 |
| Chain | Residue | Details |
| K | SER45 | |
| E | MET47 | |
| F | MET44 | |
| F | MET47 | |
| L | SER45 | |
| M | SER45 | |
| N | SER45 | |
| C | MET44 | |
| C | MET47 | |
| D | MET44 | |
| D | MET47 | |
| E | MET44 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 24 |
| Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:21183079 |
| Chain | Residue | Details |
| K | SER174 | |
| L | SER252 | |
| L | SER271 | |
| L | SER283 | |
| M | SER174 | |
| M | SER186 | |
| M | SER206 | |
| M | SER252 | |
| M | SER271 | |
| M | SER283 | |
| N | SER174 | |
| K | SER186 | |
| N | SER186 | |
| N | SER206 | |
| N | SER252 | |
| N | SER271 | |
| N | SER283 | |
| K | SER206 | |
| K | SER252 | |
| K | SER271 | |
| K | SER283 | |
| L | SER174 | |
| L | SER186 | |
| L | SER206 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | MOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P04692 |
| Chain | Residue | Details |
| K | TYR261 | |
| L | TYR261 | |
| M | TYR261 | |
| N | TYR261 | |
| E | LYS84 | |
| F | LYS84 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P19429 |
| Chain | Residue | Details |
| H | TYR27 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 4 |
| Details | MOD_RES: Phosphothreonine; by STK4/MST1 => ECO:0000250|UniProtKB:P19429 |
| Chain | Residue | Details |
| H | THR32 | |
| H | THR52 | |
| H | THR130 | |
| H | THR144 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphoserine; by PKC/PRKCE => ECO:0000269|PubMed:16445938 |
| Chain | Residue | Details |
| H | SER43 | |
| H | SER45 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P19429 |
| Chain | Residue | Details |
| H | THR79 |
| site_id | SWS_FT_FI9 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:21183079 |
| Chain | Residue | Details |
| H | SER200 |
