1C1G
CRYSTAL STRUCTURE OF TROPOMYOSIN AT 7 ANGSTROMS RESOLUTION IN THE SPERMINE-INDUCED CRYSTAL FORM
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003779 | molecular_function | actin binding |
| A | 0005856 | cellular_component | cytoskeleton |
| A | 0005884 | cellular_component | actin filament |
| A | 0007015 | biological_process | actin filament organization |
| A | 0015629 | cellular_component | actin cytoskeleton |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0042803 | molecular_function | protein homodimerization activity |
| A | 0046982 | molecular_function | protein heterodimerization activity |
| A | 0051015 | molecular_function | actin filament binding |
| A | 0060048 | biological_process | cardiac muscle contraction |
| B | 0003779 | molecular_function | actin binding |
| B | 0005856 | cellular_component | cytoskeleton |
| B | 0005884 | cellular_component | actin filament |
| B | 0007015 | biological_process | actin filament organization |
| B | 0015629 | cellular_component | actin cytoskeleton |
| B | 0042802 | molecular_function | identical protein binding |
| B | 0042803 | molecular_function | protein homodimerization activity |
| B | 0046982 | molecular_function | protein heterodimerization activity |
| B | 0051015 | molecular_function | actin filament binding |
| B | 0060048 | biological_process | cardiac muscle contraction |
| C | 0003779 | molecular_function | actin binding |
| C | 0005856 | cellular_component | cytoskeleton |
| C | 0005884 | cellular_component | actin filament |
| C | 0007015 | biological_process | actin filament organization |
| C | 0015629 | cellular_component | actin cytoskeleton |
| C | 0042802 | molecular_function | identical protein binding |
| C | 0042803 | molecular_function | protein homodimerization activity |
| C | 0046982 | molecular_function | protein heterodimerization activity |
| C | 0051015 | molecular_function | actin filament binding |
| C | 0060048 | biological_process | cardiac muscle contraction |
| D | 0003779 | molecular_function | actin binding |
| D | 0005856 | cellular_component | cytoskeleton |
| D | 0005884 | cellular_component | actin filament |
| D | 0007015 | biological_process | actin filament organization |
| D | 0015629 | cellular_component | actin cytoskeleton |
| D | 0042802 | molecular_function | identical protein binding |
| D | 0042803 | molecular_function | protein homodimerization activity |
| D | 0046982 | molecular_function | protein heterodimerization activity |
| D | 0051015 | molecular_function | actin filament binding |
| D | 0060048 | biological_process | cardiac muscle contraction |
Functional Information from PROSITE/UniProt
| site_id | PS00326 |
| Number of Residues | 9 |
| Details | TROPOMYOSIN Tropomyosins signature. LKEAEtRAE |
| Chain | Residue | Details |
| A | LEU232-GLU240 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 316 |
| Details | Region: {"description":"Disordered","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1132 |
| Details | Coiled coil: {"evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 108 |
| Details | Compositional bias: {"description":"Basic and acidic residues","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"N-acetylmethionine","evidences":[{"source":"UniProtKB","id":"P09493","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P04692","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P09493","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 16 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P58771","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"P04692","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"Phosphoserine; by DAPK1","evidences":[{"source":"UniProtKB","id":"P09493","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
