6FSA
Beta-Cardiac myosin post-rigor
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000146 | molecular_function | microfilament motor activity |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0003774 | molecular_function | cytoskeletal motor activity |
| A | 0003779 | molecular_function | actin binding |
| A | 0005516 | molecular_function | calmodulin binding |
| A | 0005524 | molecular_function | ATP binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0007512 | biological_process | adult heart development |
| A | 0016459 | cellular_component | myosin complex |
| A | 0016460 | cellular_component | myosin II complex |
| A | 0030016 | cellular_component | myofibril |
| A | 0030017 | cellular_component | sarcomere |
| A | 0030049 | biological_process | muscle filament sliding |
| A | 0032982 | cellular_component | myosin filament |
| A | 0051015 | molecular_function | actin filament binding |
| A | 0060048 | biological_process | cardiac muscle contraction |
| B | 0000146 | molecular_function | microfilament motor activity |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0003774 | molecular_function | cytoskeletal motor activity |
| B | 0003779 | molecular_function | actin binding |
| B | 0005516 | molecular_function | calmodulin binding |
| B | 0005524 | molecular_function | ATP binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0007512 | biological_process | adult heart development |
| B | 0016459 | cellular_component | myosin complex |
| B | 0016460 | cellular_component | myosin II complex |
| B | 0030016 | cellular_component | myofibril |
| B | 0030017 | cellular_component | sarcomere |
| B | 0030049 | biological_process | muscle filament sliding |
| B | 0032982 | cellular_component | myosin filament |
| B | 0051015 | molecular_function | actin filament binding |
| B | 0060048 | biological_process | cardiac muscle contraction |
| D | 0003774 | molecular_function | cytoskeletal motor activity |
| D | 0005509 | molecular_function | calcium ion binding |
| D | 0016459 | cellular_component | myosin complex |
| D | 0016460 | cellular_component | myosin II complex |
| D | 0031674 | cellular_component | I band |
| D | 0060048 | biological_process | cardiac muscle contraction |
| H | 0003774 | molecular_function | cytoskeletal motor activity |
| H | 0005509 | molecular_function | calcium ion binding |
| H | 0016459 | cellular_component | myosin complex |
| H | 0016460 | cellular_component | myosin II complex |
| H | 0031674 | cellular_component | I band |
| H | 0060048 | biological_process | cardiac muscle contraction |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | binding site for residue MG A 2001 |
| Chain | Residue |
| A | THR185 |
| A | ASN240 |
| A | SER242 |
| A | ADP2002 |
| site_id | AC2 |
| Number of Residues | 25 |
| Details | binding site for residue ADP A 2002 |
| Chain | Residue |
| A | TYR134 |
| A | GLU179 |
| A | SER180 |
| A | GLY181 |
| A | ALA182 |
| A | GLY183 |
| A | LYS184 |
| A | THR185 |
| A | VAL186 |
| A | ASN238 |
| A | MG2001 |
| A | HOH2144 |
| A | HOH2163 |
| A | HOH2167 |
| A | HOH2187 |
| A | HOH2226 |
| A | HOH2233 |
| A | HOH2276 |
| A | HOH2278 |
| A | HOH2330 |
| A | ASN126 |
| A | PRO127 |
| A | TYR128 |
| A | MLY129 |
| A | TRP130 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | binding site for residue FMT A 2003 |
| Chain | Residue |
| A | HIS251 |
| A | ARG453 |
| A | TYR455 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | binding site for residue FMT A 2004 |
| Chain | Residue |
| A | SER271 |
| A | ARG272 |
| A | PHE275 |
| A | HOH2105 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | binding site for residue EDO A 2005 |
| Chain | Residue |
| A | GLY701 |
| A | HOH2109 |
| A | HOH2300 |
| A | HOH2464 |
| site_id | AC6 |
| Number of Residues | 3 |
| Details | binding site for residue MG B 2001 |
| Chain | Residue |
| B | THR185 |
| B | SER242 |
| B | ADP2002 |
| site_id | AC7 |
| Number of Residues | 19 |
| Details | binding site for residue ADP B 2002 |
| Chain | Residue |
| B | ASN126 |
| B | PRO127 |
| B | MLY129 |
| B | TRP130 |
| B | TYR134 |
| B | GLU179 |
| B | SER180 |
| B | GLY181 |
| B | ALA182 |
| B | GLY183 |
| B | LYS184 |
| B | THR185 |
| B | VAL186 |
| B | ASN238 |
| B | MG2001 |
| B | HOH2101 |
| B | HOH2185 |
| B | HOH2238 |
| B | HOH2250 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | binding site for residue FMT B 2003 |
| Chain | Residue |
| B | GLY202 |
| B | GLU217 |
| B | LEU258 |
| B | HOH2171 |
| site_id | AC9 |
| Number of Residues | 7 |
| Details | binding site for residue FMT B 2004 |
| Chain | Residue |
| B | GLU88 |
| B | TYR117 |
| B | ARG147 |
| B | ALA150 |
| B | PRO151 |
| B | PRO152 |
| B | HOH2256 |
| site_id | AD1 |
| Number of Residues | 4 |
| Details | binding site for residue FMT B 2005 |
| Chain | Residue |
| B | TYR266 |
| B | LEU267 |
| B | THR481 |
| B | HIS651 |
| site_id | AD2 |
| Number of Residues | 7 |
| Details | binding site for residue EDO B 2006 |
| Chain | Residue |
| B | MET493 |
| B | GLY701 |
| B | ILE702 |
| B | CYS705 |
| B | HOH2116 |
| B | HOH2122 |
| B | HOH2148 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 49 |
| Details | Domain: {"description":"Myosin N-terminal SH3-like","evidences":[{"source":"PROSITE-ProRule","id":"PRU01190","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 72 |
| Details | Region: {"description":"Actin-binding","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 14 |
| Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6,N6,N6-trimethyllysine","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"P02563","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 74 |
| Details | Domain: {"description":"EF-hand 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 70 |
| Details | Domain: {"description":"EF-hand 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 64 |
| Details | Domain: {"description":"EF-hand 3","evidences":[{"evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"P16409","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI10 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"P09542","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI11 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"P16409","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI12 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P09542","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
