7PM8
Cryo-EM structure of the actomyosin-V complex in the strong-ADP state (central 1er, class 3)
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 | 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 | 1 |
Details | MOD_RES: N-acetylcysteine; in intermediate form => ECO:0000250|UniProtKB:P62737 |
Chain | Residue | Details |
C | CYS0 |
site_id | SWS_FT_FI2 |
Number of Residues | 1 |
Details | MOD_RES: N-acetylaspartate; in Actin, alpha skeletal muscle => ECO:0000269|PubMed:1150665 |
Chain | Residue | Details |
C | ASP1 |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | MOD_RES: Methionine (R)-sulfoxide => ECO:0000250|UniProtKB:P68134 |
Chain | Residue | Details |
C | MET44 | |
C | MET47 |
site_id | SWS_FT_FI4 |
Number of Residues | 1 |
Details | MOD_RES: N6-malonyllysine => ECO:0000250 |
Chain | Residue | Details |
C | LYS61 |
site_id | SWS_FT_FI5 |
Number of Residues | 1 |
Details | MOD_RES: Tele-methylhistidine => ECO:0000269|PubMed:1150665, ECO:0000269|PubMed:16905096, ECO:0000269|PubMed:213279, ECO:0000269|PubMed:2395459, ECO:0000269|PubMed:499690, ECO:0007744|PDB:1ATN, ECO:0007744|PDB:1NWK |
Chain | Residue | Details |
C | HIC73 |
site_id | SWS_FT_FI6 |
Number of Residues | 1 |
Details | MOD_RES: N6-methyllysine => ECO:0000250|UniProtKB:P68133 |
Chain | Residue | Details |
C | LYS84 |
site_id | SWS_FT_FI7 |
Number of Residues | 1 |
Details | MOD_RES: ADP-ribosylarginine; by SpvB => ECO:0000305|PubMed:16905096 |
Chain | Residue | Details |
C | ARG177 |