7UDT
cryo-EM structure of the rigor state wild type myosin-15-F-actin complex (symmetry expansion and re-centering)
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0001725 | cellular_component | stress fiber |
| A | 0005515 | molecular_function | protein binding |
| A | 0005524 | molecular_function | ATP binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005856 | cellular_component | cytoskeleton |
| A | 0005865 | cellular_component | striated muscle thin filament |
| A | 0005884 | cellular_component | actin filament |
| A | 0015629 | cellular_component | actin cytoskeleton |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0030240 | biological_process | skeletal muscle thin filament assembly |
| A | 0048741 | biological_process | skeletal muscle fiber development |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0001725 | cellular_component | stress fiber |
| B | 0005515 | molecular_function | protein binding |
| B | 0005524 | molecular_function | ATP binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005856 | cellular_component | cytoskeleton |
| B | 0005865 | cellular_component | striated muscle thin filament |
| B | 0005884 | cellular_component | actin filament |
| B | 0015629 | cellular_component | actin cytoskeleton |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0030240 | biological_process | skeletal muscle thin filament assembly |
| B | 0048741 | biological_process | skeletal muscle fiber development |
| C | 0000166 | molecular_function | nucleotide binding |
| C | 0001725 | cellular_component | stress fiber |
| C | 0005515 | molecular_function | protein binding |
| C | 0005524 | molecular_function | ATP binding |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0005856 | cellular_component | cytoskeleton |
| C | 0005865 | cellular_component | striated muscle thin filament |
| C | 0005884 | cellular_component | actin filament |
| C | 0015629 | cellular_component | actin cytoskeleton |
| C | 0016787 | molecular_function | hydrolase activity |
| C | 0030240 | biological_process | skeletal muscle thin filament assembly |
| C | 0048741 | biological_process | skeletal muscle fiber development |
| D | 0003774 | molecular_function | cytoskeletal motor activity |
| D | 0005524 | molecular_function | ATP binding |
| D | 0016459 | cellular_component | myosin complex |
| G | 0005509 | molecular_function | calcium ion binding |
Functional Information from PROSITE/UniProt
| site_id | PS00018 |
| Number of Residues | 13 |
| Details | EF_HAND_1 EF-hand calcium-binding domain. DQNRDGFIDkeDL |
| Chain | Residue | Details |
| G | ASP42-LEU54 |
| 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. WITKqEYDE |
| 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 | 35 |
| Details | Domain: {"description":"EF-hand 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 35 |
| Details | Domain: {"description":"EF-hand 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 6 |
| Details | Modified residue: {"description":"Methionine (R)-sulfoxide","evidences":[{"source":"UniProtKB","id":"P68134","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 3 |
| Details | Modified residue: {"description":"Tele-methylhistidine","evidences":[{"source":"PubMed","id":"12356759","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1MDU","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 3 |
| Details | Modified residue: {"description":"N6-methyllysine","evidences":[{"source":"UniProtKB","id":"P68133","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 22 |
| Details | Domain: {"description":"IQ 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00116","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 7 |
| Details | Region: {"description":"Actin-binding","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 27 |
| Details | Coiled coil: {"evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI10 |
| Number of Residues | 7 |
| Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
