Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

6KLL

F-actin of cardiac thin filament in low-calcium state

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	0005737	cellular_component	cytoplasm
A	0005856	cellular_component	cytoskeleton
A	0005865	cellular_component	striated muscle thin filament
A	0005884	cellular_component	actin filament
A	0010628	biological_process	positive regulation of gene expression
A	0015629	cellular_component	actin cytoskeleton
A	0016787	molecular_function	hydrolase activity
A	0030017	cellular_component	sarcomere
A	0030027	cellular_component	lamellipodium
A	0030175	cellular_component	filopodium
A	0030240	biological_process	skeletal muscle thin filament assembly
A	0032991	cellular_component	protein-containing complex
A	0044297	cellular_component	cell body
A	0048741	biological_process	skeletal muscle fiber development
A	0090131	biological_process	mesenchyme migration
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	0005737	cellular_component	cytoplasm
B	0005856	cellular_component	cytoskeleton
B	0005865	cellular_component	striated muscle thin filament
B	0005884	cellular_component	actin filament
B	0010628	biological_process	positive regulation of gene expression
B	0015629	cellular_component	actin cytoskeleton
B	0016787	molecular_function	hydrolase activity
B	0030017	cellular_component	sarcomere
B	0030027	cellular_component	lamellipodium
B	0030175	cellular_component	filopodium
B	0030240	biological_process	skeletal muscle thin filament assembly
B	0032991	cellular_component	protein-containing complex
B	0044297	cellular_component	cell body
B	0048741	biological_process	skeletal muscle fiber development
B	0090131	biological_process	mesenchyme migration
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	0005737	cellular_component	cytoplasm
C	0005856	cellular_component	cytoskeleton
C	0005865	cellular_component	striated muscle thin filament
C	0005884	cellular_component	actin filament
C	0010628	biological_process	positive regulation of gene expression
C	0015629	cellular_component	actin cytoskeleton
C	0016787	molecular_function	hydrolase activity
C	0030017	cellular_component	sarcomere
C	0030027	cellular_component	lamellipodium
C	0030175	cellular_component	filopodium
C	0030240	biological_process	skeletal muscle thin filament assembly
C	0032991	cellular_component	protein-containing complex
C	0044297	cellular_component	cell body
C	0048741	biological_process	skeletal muscle fiber development
C	0090131	biological_process	mesenchyme migration
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	0005737	cellular_component	cytoplasm
D	0005856	cellular_component	cytoskeleton
D	0005865	cellular_component	striated muscle thin filament
D	0005884	cellular_component	actin filament
D	0010628	biological_process	positive regulation of gene expression
D	0015629	cellular_component	actin cytoskeleton
D	0016787	molecular_function	hydrolase activity
D	0030017	cellular_component	sarcomere
D	0030027	cellular_component	lamellipodium
D	0030175	cellular_component	filopodium
D	0030240	biological_process	skeletal muscle thin filament assembly
D	0032991	cellular_component	protein-containing complex
D	0044297	cellular_component	cell body
D	0048741	biological_process	skeletal muscle fiber development
D	0090131	biological_process	mesenchyme migration

Functional Information from PDB Data

site_id	AC1
Number of Residues	1
Details	binding site for residue MG A 801

Chain	Residue
A	ADP802

site_id	AC2
Number of Residues	14
Details	binding site for residue ADP A 802

Chain	Residue
A	GLY301
A	GLY302
A	THR303
A	TYR306
A	LYS336
A	MG801
A	GLY13
A	SER14
A	GLY15
A	LEU16
A	LYS18
A	ASP157
A	LYS213
A	GLU214

site_id	AC3
Number of Residues	1
Details	binding site for residue MG B 801

Chain	Residue
B	ADP802

site_id	AC4
Number of Residues	14
Details	binding site for residue ADP B 802

Chain	Residue
B	GLY13
B	SER14
B	GLY15
B	LEU16
B	LYS18
B	ASP157
B	LYS213
B	GLU214
B	GLY301
B	GLY302
B	THR303
B	TYR306
B	LYS336
B	MG801

site_id	AC5
Number of Residues	1
Details	binding site for residue MG C 801

Chain	Residue
C	ADP802

site_id	AC6
Number of Residues	14
Details	binding site for residue ADP C 802

Chain	Residue
C	GLY13
C	SER14
C	GLY15
C	LEU16
C	LYS18
C	ASP157
C	LYS213
C	GLU214
C	GLY301
C	GLY302
C	THR303
C	TYR306
C	LYS336
C	MG801

site_id	AC7
Number of Residues	1
Details	binding site for residue MG D 801

Chain	Residue
D	ADP802

site_id	AC8
Number of Residues	14
Details	binding site for residue ADP D 802

Chain	Residue
D	GLY13
D	SER14
D	GLY15
D	LEU16
D	LYS18
D	ASP157
D	LYS213
D	GLU214
D	GLY301
D	GLY302
D	THR303
D	TYR306
D	LYS336
D	MG801

Functional Information from PROSITE/UniProt

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	100
Details	Region: {"description":"Interaction with alpha-actinin","evidences":[{"source":"UniProtKB","id":"P68135","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	8
Details	Modified residue: {"description":"Methionine (R)-sulfoxide","evidences":[{"source":"PubMed","id":"23911929","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	4
Details	Modified residue: {"description":"N6-malonyllysine","evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	4
Details	Modified residue: {"description":"Tele-methylhistidine","evidences":[{"source":"UniProtKB","id":"P68138","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	4
Details	Modified residue: {"description":"N6-methyllysine","evidences":[{"source":"UniProtKB","id":"P68133","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

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