7KCH
Myosin XI-F-actin complex
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 | 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 | 0016787 | molecular_function | hydrolase activity |
B | 0030240 | biological_process | skeletal muscle thin filament assembly |
B | 0048741 | biological_process | skeletal muscle fiber development |
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 | 0016787 | molecular_function | hydrolase activity |
C | 0030240 | biological_process | skeletal muscle thin filament assembly |
C | 0048741 | biological_process | skeletal muscle fiber development |
G | 0001725 | cellular_component | stress fiber |
G | 0005515 | molecular_function | protein binding |
G | 0005524 | molecular_function | ATP binding |
G | 0005737 | cellular_component | cytoplasm |
G | 0005856 | cellular_component | cytoskeleton |
G | 0005865 | cellular_component | striated muscle thin filament |
G | 0005884 | cellular_component | actin filament |
G | 0016787 | molecular_function | hydrolase activity |
G | 0030240 | biological_process | skeletal muscle thin filament assembly |
G | 0048741 | biological_process | skeletal muscle fiber development |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 13 |
Details | binding site for residue ADP G 401 |
Chain | Residue |
G | ASP11 |
G | THR303 |
G | MET305 |
G | TYR306 |
G | MG402 |
G | GLY13 |
G | LYS18 |
G | GLN137 |
G | GLY156 |
G | ASP157 |
G | LYS213 |
G | GLU214 |
G | GLY302 |
site_id | AC2 |
Number of Residues | 6 |
Details | binding site for residue MG G 402 |
Chain | Residue |
G | ASN12 |
G | GLY13 |
G | GLY15 |
G | LEU16 |
G | LYS18 |
G | ADP401 |
site_id | AC3 |
Number of Residues | 13 |
Details | binding site for residue ADP B 401 |
Chain | Residue |
B | ASP11 |
B | GLY13 |
B | LYS18 |
B | GLN137 |
B | GLY156 |
B | ASP157 |
B | LYS213 |
B | GLU214 |
B | GLY302 |
B | THR303 |
B | MET305 |
B | TYR306 |
B | MG402 |
site_id | AC4 |
Number of Residues | 6 |
Details | binding site for residue MG B 402 |
Chain | Residue |
B | ASN12 |
B | GLY13 |
B | GLY15 |
B | LEU16 |
B | LYS18 |
B | ADP401 |
site_id | AC5 |
Number of Residues | 13 |
Details | binding site for residue ADP C 401 |
Chain | Residue |
C | ASP11 |
C | GLY13 |
C | LYS18 |
C | GLN137 |
C | GLY156 |
C | ASP157 |
C | LYS213 |
C | GLU214 |
C | GLY302 |
C | THR303 |
C | MET305 |
C | TYR306 |
C | MG402 |
site_id | AC6 |
Number of Residues | 6 |
Details | binding site for residue MG C 402 |
Chain | Residue |
C | ASN12 |
C | GLY13 |
C | GLY15 |
C | LEU16 |
C | LYS18 |
C | ADP401 |
Functional Information from PROSITE/UniProt
site_id | PS00406 |
Number of Residues | 11 |
Details | ACTINS_1 Actins signature 1. YVGDEAQs.KRG |
Chain | Residue | Details |
G | TYR53-GLY63 |
site_id | PS00432 |
Number of Residues | 9 |
Details | ACTINS_2 Actins signature 2. WITKqEYDE |
Chain | Residue | Details |
G | TRP356-GLU364 |
site_id | PS01132 |
Number of Residues | 13 |
Details | ACTINS_ACT_LIKE Actins and actin-related proteins signature. LLTEApLNPkaNR |
Chain | Residue | Details |
G | LEU104-ARG116 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 3 |
Details | MOD_RES: N-acetylcysteine; in intermediate form => ECO:0000250|UniProtKB:P62737 |
Chain | Residue | Details |
G | CYS0 | |
B | CYS0 | |
C | CYS0 |
site_id | SWS_FT_FI2 |
Number of Residues | 3 |
Details | MOD_RES: N-acetylaspartate; in Actin, alpha skeletal muscle => ECO:0000269|PubMed:456601 |
Chain | Residue | Details |
G | ASP1 | |
B | ASP1 | |
C | ASP1 |
site_id | SWS_FT_FI3 |
Number of Residues | 6 |
Details | MOD_RES: Methionine (R)-sulfoxide => ECO:0000250|UniProtKB:P68134 |
Chain | Residue | Details |
G | MET44 | |
G | MET47 | |
B | MET44 | |
B | MET47 | |
C | MET44 | |
C | MET47 |
site_id | SWS_FT_FI4 |
Number of Residues | 3 |
Details | MOD_RES: Tele-methylhistidine => ECO:0000269|PubMed:12356759, ECO:0007744|PDB:1MDU |
Chain | Residue | Details |
G | HIS73 | |
B | HIS73 | |
C | HIS73 |
site_id | SWS_FT_FI5 |
Number of Residues | 3 |
Details | MOD_RES: N6-methyllysine => ECO:0000250|UniProtKB:P68133 |
Chain | Residue | Details |
G | LYS84 | |
B | LYS84 | |
C | LYS84 |