7PMF
Cryo-EM structure of the actomyosin-V complex in the post-rigor transition state (AppNHp, central 1er, class 1)
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 |
| B | 0005509 | molecular_function | calcium ion binding |
| C | 0000166 | molecular_function | nucleotide binding |
| C | 0000287 | molecular_function | magnesium ion binding |
| C | 0001725 | cellular_component | stress fiber |
| C | 0003785 | molecular_function | actin monomer binding |
| C | 0005509 | molecular_function | calcium ion binding |
| C | 0005515 | molecular_function | protein binding |
| C | 0005523 | molecular_function | tropomyosin 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 | 0010628 | biological_process | positive regulation of gene expression |
| C | 0016787 | molecular_function | hydrolase activity |
| C | 0019904 | molecular_function | protein domain specific binding |
| C | 0030027 | cellular_component | lamellipodium |
| C | 0030041 | biological_process | actin filament polymerization |
| C | 0030175 | cellular_component | filopodium |
| C | 0030240 | biological_process | skeletal muscle thin filament assembly |
| C | 0031013 | molecular_function | troponin I binding |
| C | 0031432 | molecular_function | titin binding |
| C | 0031941 | cellular_component | filamentous actin |
| C | 0032036 | molecular_function | myosin heavy chain binding |
| C | 0032432 | cellular_component | actin filament bundle |
| C | 0042802 | molecular_function | identical protein binding |
| C | 0044297 | cellular_component | cell body |
| C | 0048306 | molecular_function | calcium-dependent protein binding |
| C | 0048741 | biological_process | skeletal muscle fiber development |
| C | 0051017 | biological_process | actin filament bundle assembly |
| C | 0090131 | biological_process | mesenchyme migration |
| C | 0098723 | cellular_component | skeletal muscle myofibril |
| C | 0140660 | molecular_function | cytoskeletal motor activator activity |
Functional Information from PROSITE/UniProt
| site_id | PS00406 |
| Number of Residues | 11 |
| Details | ACTINS_1 Actins signature 1. YVGDEAQs.KRG |
| Chain | Residue | Details |
| C | TYR53-GLY63 |
| site_id | PS00432 |
| Number of Residues | 9 |
| Details | ACTINS_2 Actins signature 2. WITKqEYDE |
| Chain | Residue | Details |
| C | TRP356-GLU364 |
| site_id | PS01132 |
| Number of Residues | 13 |
| Details | ACTINS_ACT_LIKE Actins and actin-related proteins signature. LLTEApLNPkaNR |
| Chain | Residue | Details |
| C | 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 | 22 |
| Details | Domain: {"description":"IQ 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00116","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 22 |
| Details | Region: {"description":"Actin-binding","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 7 |
| Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 25 |
| Details | Region: {"description":"Interaction with alpha-actinin","evidences":[{"source":"PubMed","id":"8449927","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Methionine (R)-sulfoxide","evidences":[{"source":"UniProtKB","id":"P68134","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"N6-malonyllysine","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Tele-methylhistidine","evidences":[{"source":"PubMed","id":"1150665","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16905096","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"213279","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"2395459","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"499690","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1ATN","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1NWK","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"N6-methyllysine","evidences":[{"source":"UniProtKB","id":"P68133","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI10 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"ADP-ribosylarginine; by SpvB","evidences":[{"source":"PubMed","id":"16905096","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
