3U9D

Crystal Structure of a chimera containing the N-terminal domain (residues 8-24) of drosophila Ciboulot and the C-terminal domain (residues 13-44) of bovine Thymosin-beta4, bound to G-actin-ATP

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	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	0009612	biological_process	response to mechanical stimulus
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	0035865	biological_process	cellular response to potassium ion
A	0043503	biological_process	skeletal muscle fiber adaptation
A	0044297	cellular_component	cell body
A	0048545	biological_process	response to steroid hormone
A	0048741	biological_process	skeletal muscle fiber development
A	0090131	biological_process	mesenchyme migration
B	0003785	molecular_function	actin monomer binding
B	0007015	biological_process	actin filament organization
C	0000166	molecular_function	nucleotide binding
C	0001725	cellular_component	stress fiber
C	0005200	molecular_function	structural constituent of cytoskeleton
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	0009612	biological_process	response to mechanical stimulus
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	0035865	biological_process	cellular response to potassium ion
C	0043503	biological_process	skeletal muscle fiber adaptation
C	0044297	cellular_component	cell body
C	0048545	biological_process	response to steroid hormone
C	0048741	biological_process	skeletal muscle fiber development
C	0090131	biological_process	mesenchyme migration
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	19
Details	BINDING SITE FOR RESIDUE ATP A 501

Chain	Residue
A	GLY13
A	GLY182
A	ARG210
A	LYS213
A	GLU214
A	GLY301
A	GLY302
A	THR303
A	MET305
A	TYR306
A	MG502
A	SER14
A	GLY15
A	LEU16
A	LYS18
A	GLY156
A	ASP157
A	GLY158
A	VAL159

---

site_id	AC2
Number of Residues	2
Details	BINDING SITE FOR RESIDUE MG A 502

Chain	Residue
A	GLN137
A	ATP501

---

site_id	AC3
Number of Residues	18
Details	BINDING SITE FOR RESIDUE ATP C 501

Chain	Residue
C	GLY13
C	SER14
C	GLY15
C	LEU16
C	LYS18
C	GLN137
C	ASP154
C	GLY156
C	ASP157
C	GLY182
C	LYS213
C	GLU214
C	GLY302
C	THR303
C	MET305
C	TYR306
C	LYS336
C	MG502

---

site_id	AC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MG C 502

Chain	Residue
C	ASP11
C	GLY13
C	GLN137
C	ATP501

---

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
B	LEU30-LEU41

---

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":"UniProtKB","id":"P68135","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	2
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":"UniProtKB","id":"P68138","evidenceCode":"ECO:0000250"}]}

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":"N6-acetyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P62328","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI6
Number of Residues	4
Details	Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate","evidences":[{"source":"UniProtKB","id":"P62328","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---