Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

6M5G

F-actin-Utrophin complex

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
A	0001725	cellular_component	stress fiber
A	0005200	molecular_function	structural constituent of cytoskeleton
A	0005515	molecular_function	protein binding
A	0005524	molecular_function	ATP binding
A	0005856	cellular_component	cytoskeleton
A	0005865	cellular_component	striated muscle thin filament
A	0005884	cellular_component	actin filament
A	0015629	cellular_component	actin cytoskeleton
A	0016787	molecular_function	hydrolase activity
A	0030240	biological_process	skeletal muscle thin filament assembly
A	0048741	biological_process	skeletal muscle fiber development
B	0000166	molecular_function	nucleotide binding
B	0001725	cellular_component	stress fiber
B	0005200	molecular_function	structural constituent of cytoskeleton
B	0005515	molecular_function	protein binding
B	0005524	molecular_function	ATP binding
B	0005856	cellular_component	cytoskeleton
B	0005865	cellular_component	striated muscle thin filament
B	0005884	cellular_component	actin filament
B	0015629	cellular_component	actin cytoskeleton
B	0016787	molecular_function	hydrolase activity
B	0030240	biological_process	skeletal muscle thin filament assembly
B	0048741	biological_process	skeletal muscle fiber development
C	0000166	molecular_function	nucleotide binding
C	0001725	cellular_component	stress fiber
C	0005200	molecular_function	structural constituent of cytoskeleton
C	0005515	molecular_function	protein binding
C	0005524	molecular_function	ATP binding
C	0005856	cellular_component	cytoskeleton
C	0005865	cellular_component	striated muscle thin filament
C	0005884	cellular_component	actin filament
C	0015629	cellular_component	actin cytoskeleton
C	0016787	molecular_function	hydrolase activity
C	0030240	biological_process	skeletal muscle thin filament assembly
C	0048741	biological_process	skeletal muscle fiber development
D	0000166	molecular_function	nucleotide binding
D	0001725	cellular_component	stress fiber
D	0005200	molecular_function	structural constituent of cytoskeleton
D	0005515	molecular_function	protein binding
D	0005524	molecular_function	ATP binding
D	0005856	cellular_component	cytoskeleton
D	0005865	cellular_component	striated muscle thin filament
D	0005884	cellular_component	actin filament
D	0015629	cellular_component	actin cytoskeleton
D	0016787	molecular_function	hydrolase activity
D	0030240	biological_process	skeletal muscle thin filament assembly
D	0048741	biological_process	skeletal muscle fiber development
E	0000166	molecular_function	nucleotide binding
E	0001725	cellular_component	stress fiber
E	0005200	molecular_function	structural constituent of cytoskeleton
E	0005515	molecular_function	protein binding
E	0005524	molecular_function	ATP binding
E	0005856	cellular_component	cytoskeleton
E	0005865	cellular_component	striated muscle thin filament
E	0005884	cellular_component	actin filament
E	0015629	cellular_component	actin cytoskeleton
E	0016787	molecular_function	hydrolase activity
E	0030240	biological_process	skeletal muscle thin filament assembly
E	0048741	biological_process	skeletal muscle fiber development

Functional Information from PDB Data

site_id	AC1
Number of Residues	1
Details	binding site for residue MG A 401

Chain	Residue
A	ADP402

site_id	AC2
Number of Residues	15
Details	binding site for residue ADP A 402

Chain	Residue
A	GLU214
A	GLY301
A	GLY302
A	THR303
A	MET305
A	TYR306
A	MG401
A	GLY13
A	SER14
A	GLY15
A	LEU16
A	LYS18
A	GLY156
A	ASP157
A	LYS213

site_id	AC3
Number of Residues	1
Details	binding site for residue MG B 401

Chain	Residue
B	ADP402

site_id	AC4
Number of Residues	14
Details	binding site for residue ADP B 402

Chain	Residue
B	GLY13
B	SER14
B	GLY15
B	LEU16
B	LYS18
B	GLY156
B	ASP157
B	LYS213
B	GLU214
B	GLY302
B	THR303
B	MET305
B	TYR306
B	MG401

site_id	AC5
Number of Residues	2
Details	binding site for residue MG C 401

Chain	Residue
C	ASP154
C	ADP402

site_id	AC6
Number of Residues	14
Details	binding site for residue ADP C 402

Chain	Residue
C	GLY13
C	SER14
C	GLY15
C	LEU16
C	LYS18
C	GLY156
C	ASP157
C	LYS213
C	GLU214
C	GLY301
C	GLY302
C	TYR306
C	LYS336
C	MG401

site_id	AC7
Number of Residues	2
Details	binding site for residue MG D 401

Chain	Residue
D	ASP154
D	ADP402

site_id	AC8
Number of Residues	13
Details	binding site for residue ADP D 402

Chain	Residue
D	GLY13
D	SER14
D	GLY15
D	LEU16
D	LYS18
D	GLY156
D	ASP157
D	GLU214
D	GLY302
D	THR303
D	TYR306
D	LYS336
D	MG401

site_id	AC9
Number of Residues	2
Details	binding site for residue MG E 401

Chain	Residue
E	ASP154
E	ADP402

site_id	AD1
Number of Residues	12
Details	binding site for residue ADP E 402

Chain	Residue
E	GLY13
E	SER14
E	GLY15
E	LEU16
E	LYS18
E	GLY156
E	ASP157
E	GLU214
E	GLY302
E	THR303
E	TYR306
E	MG401

Functional Information from PROSITE/UniProt

site_id	PS00019
Number of Residues	10
Details	ACTININ_1 Actinin-type actin-binding domain signature 1. QKkTFTKWIN

Chain	Residue	Details
F	GLN33-ASN42

site_id	PS00020
Number of Residues	25
Details	ACTININ_2 Actinin-type actin-binding domain signature 2. LvNIGGtDIvDgnhkLtLGLLWsII

Chain	Residue	Details
F	LEU107-ILE131

site_id	PS00406
Number of Residues	11
Details	ACTINS_1 Actins signature 1. YVGDEAQs.KRG

Chain	Residue	Details
A	TYR53-GLY63

site_id	PS00432
Number of Residues	9
Details	ACTINS_2 Actins signature 2. WITKqEYDE

Chain	Residue	Details
A	TRP356-GLU364

site_id	PS01132
Number of Residues	13
Details	ACTINS_ACT_LIKE Actins and actin-related proteins signature. LLTEApLNPkaNR

Chain	Residue	Details
A	LEU104-ARG116

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	10
Details	Modified residue: {"description":"Methionine (R)-sulfoxide","evidences":[{"source":"UniProtKB","id":"P68134","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	5
Details	Modified residue: {"description":"Tele-methylhistidine","evidences":[{"source":"PubMed","id":"12356759","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1MDU","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	5
Details	Modified residue: {"description":"N6-methyllysine","evidences":[{"source":"UniProtKB","id":"P68133","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	312
Details	Domain: {"description":"Calponin-homology (CH) 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00044","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

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