Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

3U8X

Crystal Structure of a chimera containing the N-terminal domain (residues 8-29) of drosophila Ciboulot and the C-terminal domain (residues 18-44) of bovine Thymosin-beta4, bound to G-actin-ATP

Functional Information from GO Data

Chain	GOid	namespace	contents
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	0003785	molecular_function	actin monomer binding
B	0007015	biological_process	actin filament organization
C	0000287	molecular_function	magnesium ion binding
C	0001725	cellular_component	stress fiber
C	0003785	molecular_function	actin monomer binding
C	0005509	molecular_function	calcium ion binding
C	0005515	molecular_function	protein binding
C	0005523	molecular_function	tropomyosin 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	0016787	molecular_function	hydrolase activity
C	0019904	molecular_function	protein domain specific binding
C	0030027	cellular_component	lamellipodium
C	0030041	biological_process	actin filament polymerization
C	0030175	cellular_component	filopodium
C	0030240	biological_process	skeletal muscle thin filament assembly
C	0031013	molecular_function	troponin I binding
C	0031432	molecular_function	titin binding
C	0031941	cellular_component	filamentous actin
C	0032036	molecular_function	myosin heavy chain binding
C	0032432	cellular_component	actin filament bundle
C	0042802	molecular_function	identical protein binding
C	0044297	cellular_component	cell body
C	0048306	molecular_function	calcium-dependent protein binding
C	0048741	biological_process	skeletal muscle fiber development
C	0051017	biological_process	actin filament bundle assembly
C	0090131	biological_process	mesenchyme migration
C	0098723	cellular_component	skeletal muscle myofibril
C	0140660	molecular_function	cytoskeletal motor activator activity
D	0003785	molecular_function	actin monomer binding
D	0007015	biological_process	actin filament organization

Functional Information from PDB Data

site_id	AC1
Number of Residues	17
Details	BINDING SITE FOR RESIDUE ATP A 501

Chain	Residue
A	GLY13
A	GLU214
A	GLY301
A	GLY302
A	THR303
A	MET305
A	TYR306
A	LYS336
A	MG502
A	SER14
A	GLY15
A	LEU16
A	LYS18
A	GLY156
A	ASP157
A	ARG210
A	LYS213

site_id	AC2
Number of Residues	1
Details	BINDING SITE FOR RESIDUE MG A 502

Chain	Residue
A	ATP501

site_id	AC3
Number of Residues	20
Details	BINDING SITE FOR RESIDUE ATP C 501

Chain	Residue
C	GLY13
C	SER14
C	GLY15
C	LEU16
C	LYS18
C	GLY156
C	ASP157
C	GLY158
C	GLY182
C	ARG183
C	ARG210
C	LYS213
C	GLU214
C	GLY301
C	GLY302
C	THR303
C	MET305
C	TYR306
C	LYS336
C	MG502

site_id	AC4
Number of Residues	3
Details	BINDING SITE FOR RESIDUE MG C 502

Chain	Residue
C	GLN137
C	ASP154
C	ATP501

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
B	LEU30-LEU41

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	4
Details	MOD_RES: Phosphothreonine => ECO:0000250\|UniProtKB:P62328

Chain	Residue	Details
B	THR35
B	THR46
D	THR35
D	THR46

site_id	SWS_FT_FI2
Number of Residues	6
Details	MOD_RES: N6-acetyllysine => ECO:0000250\|UniProtKB:P62328

Chain	Residue	Details
B	LYS38
B	LYS44
B	LYS51
D	LYS38
D	LYS44
D	LYS51

site_id	SWS_FT_FI3
Number of Residues	2
Details	MOD_RES: Phosphoserine => ECO:0000250\|UniProtKB:P62328

Chain	Residue	Details
B	SER43
D	SER43

site_id	SWS_FT_FI4
Number of Residues	2
Details	MOD_RES: Tele-methylhistidine => ECO:0000269\|PubMed:1150665, ECO:0000269\|PubMed:16905096, ECO:0000269\|PubMed:213279, ECO:0000269\|PubMed:2395459, ECO:0000269\|PubMed:499690, ECO:0007744\|PDB:1ATN, ECO:0007744\|PDB:1NWK

Chain	Residue	Details
A	HIS73
C	HIS73

site_id	SWS_FT_FI5
Number of Residues	2
Details	MOD_RES: N6-methyllysine => ECO:0000250\|UniProtKB:P68133

Chain	Residue	Details
A	LYS84
C	LYS84

site_id	SWS_FT_FI6
Number of Residues	2
Details	MOD_RES: ADP-ribosylarginine; by SpvB => ECO:0000305\|PubMed:16905096

Chain	Residue	Details
A	ARG177
C	ARG177

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