Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

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

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)