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 | 4 |
Details | MOD_RES: N-acetylcysteine => ECO:0000269|PubMed:6870825 |
Chain | Residue | Details |
B | ASP2 | |
D | ASP2 | |
F | ASP2 | |
H | ASP2 |
site_id | SWS_FT_FI2 |
Number of Residues | 4 |
Details | MOD_RES: Blocked amino end (Ser) => ECO:0000269|PubMed:3312184 |
Chain | Residue | Details |
A | GLN3 | |
C | GLN3 | |
E | GLN3 | |
G | GLN3 |
site_id | SWS_FT_FI3 |
Number of Residues | 4 |
Details | MOD_RES: N6,N6,N6-trimethyllysine => ECO:0000269|PubMed:3312184 |
Chain | Residue | Details |
A | GLN129 | |
C | GLN129 | |
E | GLN129 | |
G | GLN129 |
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 |