3DTP
Tarantula heavy meromyosin obtained by flexible docking to Tarantula muscle thick filament Cryo-EM 3D-MAP
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003774 | molecular_function | cytoskeletal motor activity |
| A | 0005524 | molecular_function | ATP binding |
| A | 0016459 | cellular_component | myosin complex |
| A | 0051015 | molecular_function | actin filament binding |
| B | 0003774 | molecular_function | cytoskeletal motor activity |
| B | 0005524 | molecular_function | ATP binding |
| B | 0016459 | cellular_component | myosin complex |
| B | 0051015 | molecular_function | actin filament binding |
| C | 0000146 | molecular_function | microfilament motor activity |
| C | 0000287 | molecular_function | magnesium ion binding |
| C | 0005509 | molecular_function | calcium ion binding |
| C | 0005515 | molecular_function | protein binding |
| C | 0005829 | cellular_component | cytosol |
| C | 0005859 | cellular_component | muscle myosin complex |
| C | 0008307 | molecular_function | structural constituent of muscle |
| C | 0016459 | cellular_component | myosin complex |
| C | 0016460 | cellular_component | myosin II complex |
| C | 0030239 | biological_process | myofibril assembly |
| C | 0031032 | biological_process | actomyosin structure organization |
| C | 0032036 | molecular_function | myosin heavy chain binding |
| C | 0042641 | cellular_component | actomyosin |
| C | 0043531 | molecular_function | ADP binding |
| C | 0045159 | molecular_function | myosin II binding |
| C | 0051015 | molecular_function | actin filament binding |
| C | 0097513 | cellular_component | myosin II filament |
| D | 0000146 | molecular_function | microfilament motor activity |
| D | 0000287 | molecular_function | magnesium ion binding |
| D | 0005509 | molecular_function | calcium ion binding |
| D | 0005515 | molecular_function | protein binding |
| D | 0005829 | cellular_component | cytosol |
| D | 0005859 | cellular_component | muscle myosin complex |
| D | 0008307 | molecular_function | structural constituent of muscle |
| D | 0016459 | cellular_component | myosin complex |
| D | 0016460 | cellular_component | myosin II complex |
| D | 0030239 | biological_process | myofibril assembly |
| D | 0031032 | biological_process | actomyosin structure organization |
| D | 0032036 | molecular_function | myosin heavy chain binding |
| D | 0042641 | cellular_component | actomyosin |
| D | 0043531 | molecular_function | ADP binding |
| D | 0045159 | molecular_function | myosin II binding |
| D | 0051015 | molecular_function | actin filament binding |
| D | 0097513 | cellular_component | myosin II filament |
| E | 0005509 | molecular_function | calcium ion binding |
| E | 0009791 | biological_process | post-embryonic development |
| E | 0046872 | molecular_function | metal ion binding |
| F | 0005509 | molecular_function | calcium ion binding |
| F | 0009791 | biological_process | post-embryonic development |
| F | 0046872 | molecular_function | metal ion binding |
Functional Information from PROSITE/UniProt
| site_id | PS00018 |
| Number of Residues | 13 |
| Details | EF_HAND_1 EF-hand calcium-binding domain. DQDKDGFISknDI |
| Chain | Residue | Details |
| E | ASP67-ILE79 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 100 |
| Details | Domain: {"description":"Myosin N-terminal SH3-like","evidences":[{"source":"PROSITE-ProRule","id":"PRU01190","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 58 |
| Details | Domain: {"description":"IQ","evidences":[{"source":"PROSITE-ProRule","id":"PRU00116","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 72 |
| Details | Region: {"description":"Actin-binding"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 14 |
| Details | Binding site: {} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Blocked amino end (Ser)","evidences":[{"source":"PubMed","id":"3312184","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6,N6,N6-trimethyllysine","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"P02563","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 70 |
| Details | Domain: {"description":"EF-hand 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 70 |
| Details | Domain: {"description":"EF-hand 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI10 |
| Number of Residues | 64 |
| Details | Domain: {"description":"EF-hand 3","evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1vom |
| Chain | Residue | Details |
| B | ASN242 | |
| B | GLY180 | |
| B | GLY468 | |
| B | GLU470 |
| site_id | CSA2 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1vom |
| Chain | Residue | Details |
| A | ASN242 | |
| A | GLY180 | |
| A | GLY468 | |
| A | GLU470 |
