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 |
B | 0003774 | molecular_function | cytoskeletal motor activity |
B | 0005524 | molecular_function | ATP binding |
B | 0016459 | cellular_component | myosin complex |
B | 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 1101 |
Chain | Residue |
A | THR186 |
A | SER237 |
A | ADP1100 |
A | HOH1201 |
A | HOH1202 |
A | HOH1203 |
site_id | AC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MG B 2101 |
Chain | Residue |
B | HOH2201 |
B | HOH2203 |
B | HOH2204 |
B | THR186 |
B | SER237 |
B | ADP2100 |
site_id | AC3 |
Number of Residues | 15 |
Details | BINDING SITE FOR RESIDUE ADP A 1100 |
Chain | Residue |
A | ASN127 |
A | LYS130 |
A | TYR135 |
A | GLU180 |
A | GLY182 |
A | ALA183 |
A | GLY184 |
A | LYS185 |
A | THR186 |
A | GLU187 |
A | ASN233 |
A | MG1101 |
A | HOH1201 |
A | HOH1203 |
A | HOH1205 |
site_id | AC4 |
Number of Residues | 16 |
Details | BINDING SITE FOR RESIDUE ADP B 2100 |
Chain | Residue |
B | ASN127 |
B | PRO128 |
B | LYS130 |
B | ARG131 |
B | TYR135 |
B | GLU180 |
B | GLY182 |
B | ALA183 |
B | GLY184 |
B | LYS185 |
B | THR186 |
B | GLU187 |
B | ASN233 |
B | MG2101 |
B | HOH2203 |
B | HOH2204 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | BINDING: |
Chain | Residue | Details |
A | GLY179 | |
B | GLY179 | |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | MOD_RES: N6,N6-dimethyllysine => ECO:0000255 |
Chain | Residue | Details |
A | LYS130 | |
B | LYS130 | |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1vom |
Chain | Residue | Details |
A | GLU459 | |
A | GLY182 | |
A | GLY457 | |
A | ASN233 | |
site_id | CSA2 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1vom |
Chain | Residue | Details |
B | GLU459 | |
B | GLY182 | |
B | GLY457 | |
B | ASN233 | |
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 | GLU459 | electrostatic stabiliser, proton acceptor, proton donor |
site_id | MCSA2 |
Number of Residues | 8 |
Details | M-CSA 534 |
Chain | Residue | Details |
B | SER181 | proton acceptor, proton donor, proton relay |
B | GLY182 | electrostatic stabiliser |
B | THR186 | metal ligand |
B | ASN233 | electrostatic stabiliser |
B | SER236 | proton acceptor, proton donor, proton relay |
B | SER237 | metal ligand |
B | GLY457 | electrostatic stabiliser |
B | GLU459 | electrostatic stabiliser, proton acceptor, proton donor |