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 |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | binding site for residue MG A 801 |
| Chain | Residue |
| A | THR186 |
| A | SER237 |
| A | ADP802 |
| A | HOH911 |
| A | HOH955 |
| A | HOH902 |
| site_id | AC2 |
| Number of Residues | 23 |
| Details | binding site for residue ADP A 802 |
| Chain | Residue |
| A | LYS130 |
| A | TYR135 |
| A | GLU180 |
| A | GLY182 |
| A | ALA183 |
| A | GLY184 |
| A | LYS185 |
| A | THR186 |
| A | GLU187 |
| A | ASN233 |
| A | MG801 |
| A | PO4803 |
| A | HOH911 |
| A | HOH955 |
| A | HOH902 |
| A | HOH925 |
| A | HOH1116 |
| A | HOH1092 |
| A | HOH1107 |
| A | HOH1113 |
| A | ASN127 |
| A | PRO128 |
| A | PHE129 |
| site_id | AC3 |
| Number of Residues | 10 |
| Details | binding site for residue PO4 A 803 |
| Chain | Residue |
| A | GLU180 |
| A | SER181 |
| A | LYS185 |
| A | SER237 |
| A | SER456 |
| A | GLY457 |
| A | ARG459 |
| A | ADP802 |
| A | HOH902 |
| A | HOH922 |
| site_id | AC4 |
| Number of Residues | 7 |
| Details | binding site for residue PO4 A 804 |
| Chain | Residue |
| A | GLU180 |
| A | ASN660 |
| A | VAL671 |
| A | ASP674 |
| A | GLN675 |
| A | GOL805 |
| A | HOH1146 |
| site_id | AC5 |
| Number of Residues | 9 |
| Details | binding site for residue GOL A 805 |
| Chain | Residue |
| A | GLU180 |
| A | TYR573 |
| A | GLN675 |
| A | ASN679 |
| A | PO4804 |
| A | HOH921 |
| A | HOH954 |
| A | HOH919 |
| A | HOH1146 |
| site_id | AC6 |
| Number of Residues | 7 |
| Details | binding site for residue GOL A 806 |
| Chain | Residue |
| A | LYS265 |
| A | LYS423 |
| A | ALA424 |
| A | LEU431 |
| A | HOH932 |
| A | HOH1055 |
| A | HOH956 |
| site_id | AC7 |
| Number of Residues | 8 |
| Details | binding site for residue GOL A 807 |
| Chain | Residue |
| A | ILE35 |
| A | TRP36 |
| A | TYR37 |
| A | ASN38 |
| A | TYR47 |
| A | ASP76 |
| A | ASN78 |
| A | HOH1076 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | binding site for residue GOL A 808 |
| Chain | Residue |
| A | LYS16 |
| A | GLU89 |
| A | ASN149 |
| A | VAL151 |
| A | ALA152 |
| A | HOH1183 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | binding site for residue GOL A 809 |
| Chain | Residue |
| A | LYS42 |
| A | SER549 |
| A | HIS550 |
| A | LYS554 |
| site_id | AD1 |
| Number of Residues | 6 |
| Details | binding site for residue GOL A 810 |
| Chain | Residue |
| A | PRO220 |
| A | GLU223 |
| A | ALA224 |
| A | ASN235 |
| A | HIS279 |
| A | HOH970 |
| site_id | AD2 |
| Number of Residues | 8 |
| Details | binding site for residue GOL A 811 |
| Chain | Residue |
| A | GLN19 |
| A | GLY20 |
| A | PHE25 |
| A | ARG397 |
| A | ILE398 |
| A | LEU399 |
| A | GLN594 |
| A | HOH976 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 52 |
| Details | Domain: {"description":"Myosin N-terminal SH3-like","evidences":[{"source":"PROSITE-ProRule","id":"PRU01190","evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 22 |
| Details | Region: {"description":"Actin-binding"} |
| site_id | SWS_FT_FI3 |
| Number of Residues | 7 |
| Details | Binding site: {} |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"N6,N6-dimethyllysine","evidences":[{"evidenceCode":"ECO:0000255"}]} |
Catalytic Information from CSA
| site_id | MCSA1 |
| Number of Residues | 8 |
| Details | M-CSA 534 |
| Chain | Residue | Details |
| A | SER181 | proton acceptor, proton donor, proton relay |
| A | GLY182 | electrostatic stabiliser |
| A | THR186 | metal ligand |
| A | ASN233 | electrostatic stabiliser |
| A | SER236 | proton acceptor, proton donor, proton relay |
| A | SER237 | metal ligand |
| A | GLY457 | electrostatic stabiliser |
| A | ARG459 | electrostatic stabiliser, proton acceptor, proton donor |