Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

6JBK

Crystal structure of an actin monomer in complex with the nucleator Cordon-Bleu WH2-motif peptide mutant. T22V

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	0003779	molecular_function	actin binding
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	0003779	molecular_function	actin binding
E	0000287	molecular_function	magnesium ion binding
E	0001725	cellular_component	stress fiber
E	0003785	molecular_function	actin monomer binding
E	0005509	molecular_function	calcium ion binding
E	0005515	molecular_function	protein binding
E	0005523	molecular_function	tropomyosin binding
E	0005524	molecular_function	ATP binding
E	0005737	cellular_component	cytoplasm
E	0005856	cellular_component	cytoskeleton
E	0005865	cellular_component	striated muscle thin filament
E	0005884	cellular_component	actin filament
E	0010628	biological_process	positive regulation of gene expression
E	0016787	molecular_function	hydrolase activity
E	0019904	molecular_function	protein domain specific binding
E	0030027	cellular_component	lamellipodium
E	0030041	biological_process	actin filament polymerization
E	0030175	cellular_component	filopodium
E	0030240	biological_process	skeletal muscle thin filament assembly
E	0031013	molecular_function	troponin I binding
E	0031432	molecular_function	titin binding
E	0031941	cellular_component	filamentous actin
E	0032036	molecular_function	myosin heavy chain binding
E	0032432	cellular_component	actin filament bundle
E	0042802	molecular_function	identical protein binding
E	0044297	cellular_component	cell body
E	0048306	molecular_function	calcium-dependent protein binding
E	0048741	biological_process	skeletal muscle fiber development
E	0051017	biological_process	actin filament bundle assembly
E	0090131	biological_process	mesenchyme migration
E	0098723	cellular_component	skeletal muscle myofibril
E	0140660	molecular_function	cytoskeletal motor activator activity
F	0003779	molecular_function	actin binding
G	0000287	molecular_function	magnesium ion binding
G	0001725	cellular_component	stress fiber
G	0003785	molecular_function	actin monomer binding
G	0005509	molecular_function	calcium ion binding
G	0005515	molecular_function	protein binding
G	0005523	molecular_function	tropomyosin binding
G	0005524	molecular_function	ATP binding
G	0005737	cellular_component	cytoplasm
G	0005856	cellular_component	cytoskeleton
G	0005865	cellular_component	striated muscle thin filament
G	0005884	cellular_component	actin filament
G	0010628	biological_process	positive regulation of gene expression
G	0016787	molecular_function	hydrolase activity
G	0019904	molecular_function	protein domain specific binding
G	0030027	cellular_component	lamellipodium
G	0030041	biological_process	actin filament polymerization
G	0030175	cellular_component	filopodium
G	0030240	biological_process	skeletal muscle thin filament assembly
G	0031013	molecular_function	troponin I binding
G	0031432	molecular_function	titin binding
G	0031941	cellular_component	filamentous actin
G	0032036	molecular_function	myosin heavy chain binding
G	0032432	cellular_component	actin filament bundle
G	0042802	molecular_function	identical protein binding
G	0044297	cellular_component	cell body
G	0048306	molecular_function	calcium-dependent protein binding
G	0048741	biological_process	skeletal muscle fiber development
G	0051017	biological_process	actin filament bundle assembly
G	0090131	biological_process	mesenchyme migration
G	0098723	cellular_component	skeletal muscle myofibril
G	0140660	molecular_function	cytoskeletal motor activator activity
H	0003779	molecular_function	actin binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	26
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	HOH526
A	HOH547
A	HOH566
A	HOH569
A	HOH572
A	HOH582
A	HOH584
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	HOH523
A	HOH538
A	HOH554
A	HOH566
A	HOH569

site_id	AC3
Number of Residues	4
Details	binding site for residue CA A 403

Chain	Residue
A	ASP286
A	ASP288
A	HOH590
G	ASP363

site_id	AC4
Number of Residues	26
Details	binding site for residue ATP C 401

Chain	Residue
C	GLY13
C	SER14
C	GLY15
C	LEU16
C	LYS18
C	GLY156
C	ASP157
C	GLY158
C	VAL159
C	GLY182
C	LYS213
C	GLU214
C	GLY301
C	GLY302
C	THR303
C	MET305
C	TYR306
C	LYS336
C	CA402
C	HOH526
C	HOH538
C	HOH540
C	HOH559
C	HOH569
C	HOH579
C	HOH593

site_id	AC5
Number of Residues	6
Details	binding site for residue CA C 402

Chain	Residue
C	ATP401
C	HOH537
C	HOH540
C	HOH549
C	HOH552
C	HOH569

site_id	AC6
Number of Residues	5
Details	binding site for residue CA C 403

Chain	Residue
C	ASP286
C	ASP288
C	HOH592
E	ASP363
E	HOH574

site_id	AC7
Number of Residues	27
Details	binding site for residue ATP E 401

Chain	Residue
E	HOH564
E	GLY13
E	SER14
E	GLY15
E	LEU16
E	LYS18
E	GLY156
E	ASP157
E	GLY158
E	VAL159
E	GLY182
E	ARG210
E	LYS213
E	GLU214
E	GLY301
E	GLY302
E	THR303
E	MET305
E	TYR306
E	LYS336
E	CA402
E	HOH539
E	HOH541
E	HOH545
E	HOH554
E	HOH556
E	HOH558

site_id	AC8
Number of Residues	6
Details	binding site for residue CA E 402

Chain	Residue
E	ATP401
E	HOH520
E	HOH527
E	HOH539
E	HOH541
E	HOH545

site_id	AC9
Number of Residues	5
Details	binding site for residue CA E 403

Chain	Residue
C	ASP363
C	HOH577
E	ASP286
E	ASP288
E	HOH580

site_id	AD1
Number of Residues	25
Details	binding site for residue ATP G 401

Chain	Residue
G	GLY13
G	SER14
G	GLY15
G	LEU16
G	LYS18
G	GLY156
G	ASP157
G	GLY158
G	VAL159
G	GLY182
G	ARG210
G	LYS213
G	GLU214
G	GLY301
G	GLY302
G	THR303
G	MET305
G	TYR306
G	LYS336
G	CA402
G	HOH503
G	HOH534
G	HOH536
G	HOH542
G	HOH549

site_id	AD2
Number of Residues	6
Details	binding site for residue CA G 402

Chain	Residue
G	ATP401
G	HOH523
G	HOH527
G	HOH529
G	HOH536
G	HOH549

site_id	AD3
Number of Residues	5
Details	binding site for residue CA G 403

Chain	Residue
A	ASP363
A	HOH555
G	ASP286
G	ASP288
G	HOH580

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	4
Details	MOD_RES: N-acetylcysteine; in intermediate form => ECO:0000250\|UniProtKB:P62737

Chain	Residue	Details
A	CYS0
C	CYS0
E	CYS0
G	CYS0

site_id	SWS_FT_FI2
Number of Residues	4
Details	MOD_RES: N-acetylaspartate; in Actin, alpha skeletal muscle => ECO:0000269\|PubMed:1150665

Chain	Residue	Details
A	ASP1
C	ASP1
E	ASP1
G	ASP1

site_id	SWS_FT_FI3
Number of Residues	8
Details	MOD_RES: Methionine (R)-sulfoxide => ECO:0000250\|UniProtKB:P68134

Chain	Residue	Details
A	MET44
A	MET47
C	MET44
C	MET47
E	MET44
E	MET47
G	MET44
G	MET47

site_id	SWS_FT_FI4
Number of Residues	4
Details	MOD_RES: N6-malonyllysine => ECO:0000250

Chain	Residue	Details
A	LYS61
C	LYS61
E	LYS61
G	LYS61

site_id	SWS_FT_FI5
Number of Residues	4
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	HIC73
C	HIC73
E	HIC73
G	HIC73

site_id	SWS_FT_FI6
Number of Residues	4
Details	MOD_RES: N6-methyllysine => ECO:0000250\|UniProtKB:P68133

Chain	Residue	Details
A	LYS84
C	LYS84
E	LYS84
G	LYS84

site_id	SWS_FT_FI7
Number of Residues	4
Details	MOD_RES: ADP-ribosylarginine; by SpvB => ECO:0000305\|PubMed:16905096

Chain	Residue	Details
A	ARG177
C	ARG177
E	ARG177
G	ARG177

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