1BR4
SMOOTH MUSCLE MYOSIN MOTOR DOMAIN-ESSENTIAL LIGHT CHAIN COMPLEX WITH MGADP.BEF3 BOUND AT THE ACTIVE SITE
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 | 0000146 | molecular_function | microfilament motor activity |
| B | 0000287 | molecular_function | magnesium ion binding |
| B | 0005509 | molecular_function | calcium ion binding |
| B | 0005515 | molecular_function | protein binding |
| B | 0005829 | cellular_component | cytosol |
| B | 0005859 | cellular_component | muscle myosin complex |
| B | 0008307 | molecular_function | structural constituent of muscle |
| B | 0016459 | cellular_component | myosin complex |
| B | 0016460 | cellular_component | myosin II complex |
| B | 0030239 | biological_process | myofibril assembly |
| B | 0031032 | biological_process | actomyosin structure organization |
| B | 0032036 | molecular_function | myosin heavy chain binding |
| B | 0042641 | cellular_component | actomyosin |
| B | 0043531 | molecular_function | ADP binding |
| B | 0045159 | molecular_function | myosin II binding |
| B | 0051015 | molecular_function | actin filament binding |
| B | 0097513 | cellular_component | myosin II filament |
| C | 0003774 | molecular_function | cytoskeletal motor activity |
| C | 0005524 | molecular_function | ATP binding |
| C | 0016459 | cellular_component | myosin complex |
| C | 0051015 | molecular_function | actin filament binding |
| D | 0000146 | molecular_function | microfilament motor activity |
| D | 0000287 | molecular_function | magnesium ion binding |
| D | 0005509 | molecular_function | calcium ion binding |
| D | 0005515 | molecular_function | protein binding |
| D | 0005829 | cellular_component | cytosol |
| D | 0005859 | cellular_component | muscle myosin complex |
| D | 0008307 | molecular_function | structural constituent of muscle |
| D | 0016459 | cellular_component | myosin complex |
| D | 0016460 | cellular_component | myosin II complex |
| D | 0030239 | biological_process | myofibril assembly |
| D | 0031032 | biological_process | actomyosin structure organization |
| D | 0032036 | molecular_function | myosin heavy chain binding |
| D | 0042641 | cellular_component | actomyosin |
| D | 0043531 | molecular_function | ADP binding |
| D | 0045159 | molecular_function | myosin II binding |
| D | 0051015 | molecular_function | actin filament binding |
| D | 0097513 | cellular_component | myosin II filament |
| E | 0003774 | molecular_function | cytoskeletal motor activity |
| E | 0005524 | molecular_function | ATP binding |
| E | 0016459 | cellular_component | myosin complex |
| E | 0051015 | molecular_function | actin filament binding |
| F | 0000146 | molecular_function | microfilament motor activity |
| F | 0000287 | molecular_function | magnesium ion binding |
| F | 0005509 | molecular_function | calcium ion binding |
| F | 0005515 | molecular_function | protein binding |
| F | 0005829 | cellular_component | cytosol |
| F | 0005859 | cellular_component | muscle myosin complex |
| F | 0008307 | molecular_function | structural constituent of muscle |
| F | 0016459 | cellular_component | myosin complex |
| F | 0016460 | cellular_component | myosin II complex |
| F | 0030239 | biological_process | myofibril assembly |
| F | 0031032 | biological_process | actomyosin structure organization |
| F | 0032036 | molecular_function | myosin heavy chain binding |
| F | 0042641 | cellular_component | actomyosin |
| F | 0043531 | molecular_function | ADP binding |
| F | 0045159 | molecular_function | myosin II binding |
| F | 0051015 | molecular_function | actin filament binding |
| F | 0097513 | cellular_component | myosin II filament |
| G | 0003774 | molecular_function | cytoskeletal motor activity |
| G | 0005524 | molecular_function | ATP binding |
| G | 0016459 | cellular_component | myosin complex |
| G | 0051015 | molecular_function | actin filament binding |
| H | 0000146 | molecular_function | microfilament motor activity |
| H | 0000287 | molecular_function | magnesium ion binding |
| H | 0005509 | molecular_function | calcium ion binding |
| H | 0005515 | molecular_function | protein binding |
| H | 0005829 | cellular_component | cytosol |
| H | 0005859 | cellular_component | muscle myosin complex |
| H | 0008307 | molecular_function | structural constituent of muscle |
| H | 0016459 | cellular_component | myosin complex |
| H | 0016460 | cellular_component | myosin II complex |
| H | 0030239 | biological_process | myofibril assembly |
| H | 0031032 | biological_process | actomyosin structure organization |
| H | 0032036 | molecular_function | myosin heavy chain binding |
| H | 0042641 | cellular_component | actomyosin |
| H | 0043531 | molecular_function | ADP binding |
| H | 0045159 | molecular_function | myosin II binding |
| H | 0051015 | molecular_function | actin filament binding |
| H | 0097513 | cellular_component | myosin II filament |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG A 997 |
| Chain | Residue |
| A | THR184 |
| A | SER246 |
| A | ASP465 |
| A | HOH995 |
| A | ADP998 |
| A | BEF999 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG C 997 |
| Chain | Residue |
| C | HOH995 |
| C | ADP998 |
| C | BEF999 |
| C | THR184 |
| C | SER246 |
| C | ASP465 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG E 997 |
| Chain | Residue |
| E | THR184 |
| E | SER246 |
| E | ASP465 |
| E | HOH995 |
| E | ADP998 |
| E | BEF999 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG G 997 |
| Chain | Residue |
| G | THR184 |
| G | SER246 |
| G | ASP465 |
| G | HOH995 |
| G | ADP998 |
| G | BEF999 |
| site_id | AC5 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE ADP A 998 |
| Chain | Residue |
| A | ASN125 |
| A | PRO126 |
| A | TYR127 |
| A | LYS128 |
| A | TYR133 |
| A | GLY180 |
| A | ALA181 |
| A | GLY182 |
| A | LYS183 |
| A | THR184 |
| A | GLU185 |
| A | ASN242 |
| A | HOH995 |
| A | HOH996 |
| A | MG997 |
| A | BEF999 |
| site_id | AC6 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE BEF A 999 |
| Chain | Residue |
| A | SER179 |
| A | GLY180 |
| A | LYS183 |
| A | ASN242 |
| A | SER245 |
| A | SER246 |
| A | GLY468 |
| A | HOH995 |
| A | MG997 |
| A | ADP998 |
| site_id | AC7 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE ADP C 998 |
| Chain | Residue |
| C | ASN125 |
| C | PRO126 |
| C | TYR127 |
| C | LYS128 |
| C | TYR133 |
| C | GLY180 |
| C | ALA181 |
| C | GLY182 |
| C | LYS183 |
| C | THR184 |
| C | GLU185 |
| C | ASN242 |
| C | HOH995 |
| C | HOH996 |
| C | MG997 |
| C | BEF999 |
| site_id | AC8 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE BEF C 999 |
| Chain | Residue |
| C | SER179 |
| C | GLY180 |
| C | LYS183 |
| C | ASN242 |
| C | SER245 |
| C | SER246 |
| C | GLY468 |
| C | HOH995 |
| C | MG997 |
| C | ADP998 |
| site_id | AC9 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE ADP E 998 |
| Chain | Residue |
| E | ASN125 |
| E | PRO126 |
| E | TYR127 |
| E | LYS128 |
| E | TYR133 |
| E | GLY180 |
| E | ALA181 |
| E | GLY182 |
| E | LYS183 |
| E | THR184 |
| E | GLU185 |
| E | ASN242 |
| E | HOH995 |
| E | HOH996 |
| E | MG997 |
| E | BEF999 |
| site_id | BC1 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE BEF E 999 |
| Chain | Residue |
| E | HOH995 |
| E | MG997 |
| E | ADP998 |
| E | SER179 |
| E | GLY180 |
| E | LYS183 |
| E | ASN242 |
| E | SER245 |
| E | SER246 |
| E | GLY468 |
| site_id | BC2 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE ADP G 998 |
| Chain | Residue |
| G | ASN125 |
| G | PRO126 |
| G | TYR127 |
| G | LYS128 |
| G | TYR133 |
| G | GLY180 |
| G | ALA181 |
| G | GLY182 |
| G | LYS183 |
| G | THR184 |
| G | GLU185 |
| G | ASN242 |
| G | HOH995 |
| G | HOH996 |
| G | MG997 |
| G | BEF999 |
| site_id | BC3 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE BEF G 999 |
| Chain | Residue |
| G | SER179 |
| G | GLY180 |
| G | LYS183 |
| G | ASN242 |
| G | SER245 |
| G | SER246 |
| G | GLY468 |
| G | HOH995 |
| G | MG997 |
| G | ADP998 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 200 |
| 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 | 144 |
| Details | Region: {"description":"Actin-binding"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 28 |
| Details | Binding site: {} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"Blocked amino end (Ser)","evidences":[{"source":"PubMed","id":"3312184","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"N6,N6,N6-trimethyllysine","evidences":[{"source":"PubMed","id":"3312184","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 140 |
| 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 | 140 |
| 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 | 128 |
| Details | Domain: {"description":"EF-hand 3","evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1vom |
| Chain | Residue | Details |
| A | ASN242 | |
| A | GLY180 | |
| A | GLY468 | |
| A | GLU470 |
| site_id | CSA2 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1vom |
| Chain | Residue | Details |
| C | ASN242 | |
| C | GLY180 | |
| C | GLY468 | |
| C | GLU470 |
| site_id | CSA3 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1vom |
| Chain | Residue | Details |
| E | ASN242 | |
| E | GLY180 | |
| E | GLY468 | |
| E | GLU470 |
| site_id | CSA4 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1vom |
| Chain | Residue | Details |
| G | ASN242 | |
| G | GLY180 | |
| G | GLY468 | |
| G | GLU470 |
