Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

4PL8

Structure of rabbit skeletal muscle actin in complex with a hybrid peptide comprising thymosin beta4 and the lysine-rich region of Cordon-Bleu

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
A	0000287	molecular_function	magnesium ion binding
A	0001725	cellular_component	stress fiber
A	0003785	molecular_function	actin monomer binding
A	0005509	molecular_function	calcium ion binding
A	0005515	molecular_function	protein binding
A	0005523	molecular_function	tropomyosin 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	0016787	molecular_function	hydrolase activity
A	0019904	molecular_function	protein domain specific binding
A	0030027	cellular_component	lamellipodium
A	0030041	biological_process	actin filament polymerization
A	0030175	cellular_component	filopodium
A	0030240	biological_process	skeletal muscle thin filament assembly
A	0031013	molecular_function	troponin I binding
A	0031432	molecular_function	titin binding
A	0031941	cellular_component	filamentous actin
A	0032036	molecular_function	myosin heavy chain binding
A	0032432	cellular_component	actin filament bundle
A	0042802	molecular_function	identical protein binding
A	0044297	cellular_component	cell body
A	0048306	molecular_function	calcium-dependent protein binding
A	0048741	biological_process	skeletal muscle fiber development
A	0051017	biological_process	actin filament bundle assembly
A	0090131	biological_process	mesenchyme migration
A	0098723	cellular_component	skeletal muscle myofibril
A	0140660	molecular_function	cytoskeletal motor activator activity
B	0000166	molecular_function	nucleotide binding
B	0000287	molecular_function	magnesium ion binding
B	0001725	cellular_component	stress fiber
B	0003785	molecular_function	actin monomer binding
B	0005509	molecular_function	calcium ion binding
B	0005515	molecular_function	protein binding
B	0005523	molecular_function	tropomyosin 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	0016787	molecular_function	hydrolase activity
B	0019904	molecular_function	protein domain specific binding
B	0030027	cellular_component	lamellipodium
B	0030041	biological_process	actin filament polymerization
B	0030175	cellular_component	filopodium
B	0030240	biological_process	skeletal muscle thin filament assembly
B	0031013	molecular_function	troponin I binding
B	0031432	molecular_function	titin binding
B	0031941	cellular_component	filamentous actin
B	0032036	molecular_function	myosin heavy chain binding
B	0032432	cellular_component	actin filament bundle
B	0042802	molecular_function	identical protein binding
B	0044297	cellular_component	cell body
B	0048306	molecular_function	calcium-dependent protein binding
B	0048741	biological_process	skeletal muscle fiber development
B	0051017	biological_process	actin filament bundle assembly
B	0090131	biological_process	mesenchyme migration
B	0098723	cellular_component	skeletal muscle myofibril
B	0140660	molecular_function	cytoskeletal motor activator activity
H	0003723	molecular_function	RNA binding
H	0003779	molecular_function	actin binding
H	0003785	molecular_function	actin monomer binding
H	0003788	molecular_function	actin monomer sequestering activity
H	0005515	molecular_function	protein binding
H	0005576	cellular_component	extracellular region
H	0005634	cellular_component	nucleus
H	0005737	cellular_component	cytoplasm
H	0005829	cellular_component	cytosol
H	0005856	cellular_component	cytoskeleton
H	0007015	biological_process	actin filament organization
H	0019899	molecular_function	enzyme binding
H	0030334	biological_process	regulation of cell migration
H	0030837	biological_process	negative regulation of actin filament polymerization
H	0031093	cellular_component	platelet alpha granule lumen
H	0033209	biological_process	tumor necrosis factor-mediated signaling pathway
H	0043124	biological_process	negative regulation of canonical NF-kappaB signal transduction
H	0043536	biological_process	positive regulation of blood vessel endothelial cell migration
H	0050728	biological_process	negative regulation of inflammatory response
H	0140311	molecular_function	protein sequestering activity
H	2001028	biological_process	positive regulation of endothelial cell chemotaxis
H	2001171	biological_process	positive regulation of ATP biosynthetic process

Functional Information from PDB Data

site_id	AC1
Number of Residues	27
Details	binding site for residue ATP A 401

Chain	Residue
A	GLY13
A	GLY182
A	LYS213
A	GLU214
A	GLY301
A	GLY302
A	THR303
A	MET305
A	TYR306
A	LYS336
A	CA402
A	SER14
A	HOH565
A	HOH567
A	HOH568
A	HOH569
A	HOH570
A	HOH598
A	HOH729
A	HOH755
A	GLY15
A	LEU16
A	LYS18
A	GLY156
A	ASP157
A	GLY158
A	VAL159

site_id	AC2
Number of Residues	6
Details	binding site for residue CA A 402

Chain	Residue
A	ATP401
A	HOH563
A	HOH564
A	HOH566
A	HOH567
A	HOH568

site_id	AC3
Number of Residues	25
Details	binding site for residue ATP B 401

Chain	Residue
B	GLY13
B	SER14
B	GLY15
B	LEU16
B	LYS18
B	GLY156
B	ASP157
B	GLY158
B	VAL159
B	GLY182
B	ARG210
B	LYS213
B	GLU214
B	GLY301
B	GLY302
B	THR303
B	MET305
B	TYR306
B	CA402
B	HOH550
B	HOH552
B	HOH580
B	HOH656
B	HOH662
B	HOH667

site_id	AC4
Number of Residues	6
Details	binding site for residue CA B 402

Chain	Residue
B	ATP401
B	HOH550
B	HOH551
B	HOH552
B	HOH554
B	HOH639

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	PS00500
Number of Residues	12
Details	THYMOSIN_B4 Thymosin beta-4 family signature. LKKTETqeKNPL

Chain	Residue	Details
H	LEU47-LEU58

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	50
Details	Region: {"description":"Interaction with alpha-actinin","evidences":[{"source":"PubMed","id":"8449927","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	1
Details	Modified residue: {"description":"N6-malonyllysine","evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	2
Details	Modified residue: {"description":"Tele-methylhistidine","evidences":[{"source":"PubMed","id":"1150665","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16905096","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"213279","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"2395459","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"499690","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1ATN","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1NWK","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	2
Details	Modified residue: {"description":"N6-methyllysine","evidences":[{"source":"UniProtKB","id":"P68133","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	2
Details	Modified residue: {"description":"ADP-ribosylarginine; by SpvB","evidences":[{"source":"PubMed","id":"16905096","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	1
Details	Modified residue: {"description":"N6-acetyllysine; alternate","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	1
Details	Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	1
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI9
Number of Residues	2
Details	Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate","evidences":[{"source":"PubMed","id":"28112733","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)