Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

3FFK

Crystal structure of human Gelsolin domains G1-G3 bound to Actin

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0051015	molecular_function	actin filament 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
D	0051015	molecular_function	actin filament 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

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA A 756

Chain	Residue
A	GLY186
A	ASP187
A	GLU209
A	ASP259
A	HOH789
A	HOH883

site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CA A 757

Chain	Residue
A	VAL145
A	GLY65
A	ASP66
A	GLU97

site_id	AC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA A 758

Chain	Residue
A	ASP109
A	GLY114
A	ALA116
A	HOH853
A	HOH882
B	GLU167

site_id	AC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CA A 759

Chain	Residue
A	GLU302
A	ASP303
A	GLU327
A	HOH777
A	HOH802

site_id	AC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CA B 401

Chain	Residue
B	ATP380
B	HOH392
B	HOH398
B	HOH469
B	HOH470

site_id	AC6
Number of Residues	22
Details	BINDING SITE FOR RESIDUE ATP B 380

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	HOH379
B	HOH392
B	CA401
B	HOH470

site_id	AC7
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA D 756

Chain	Residue
D	GLY186
D	ASP187
D	GLU209
D	ASP259
D	HOH784
D	HOH852

site_id	AC8
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CA D 757

Chain	Residue
D	GLY65
D	ASP66
D	GLU97
D	VAL145

site_id	AC9
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CA D 758

Chain	Residue
D	ASP109
D	GLY114
D	ALA116
D	HOH833
E	GLU167

site_id	BC1
Number of Residues	3
Details	BINDING SITE FOR RESIDUE CA D 759

Chain	Residue
D	GLU302
D	ASP303
D	GLU327

site_id	BC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CA E 401

Chain	Residue
E	ATP380
E	HOH395
E	HOH433
E	HOH441
E	HOH490

site_id	BC3
Number of Residues	23
Details	BINDING SITE FOR RESIDUE ATP E 380

Chain	Residue
E	GLY13
E	SER14
E	GLY15
E	LEU16
E	LYS18
E	GLY156
E	ASP157
E	GLY158
E	VAL159
E	GLY182
E	LYS213
E	GLU214
E	GLY301
E	GLY302
E	THR303
E	MET305
E	TYR306
E	HOH395
E	CA401
E	HOH440
E	HOH450
E	HOH490
E	HOH495

Functional Information from PROSITE/UniProt

site_id	PS00406
Number of Residues	11
Details	ACTINS_1 Actins signature 1. YVGDEAQs.KRG

Chain	Residue	Details
B	TYR53-GLY63

site_id	PS00432
Number of Residues	9
Details	ACTINS_2 Actins signature 2. WITKqEYDE

Chain	Residue	Details
B	TRP356-GLU364

site_id	PS01132
Number of Residues	13
Details	ACTINS_ACT_LIKE Actins and actin-related proteins signature. LLTEApLNPkaNR

Chain	Residue	Details
B	LEU104-ARG116

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	MOD_RES: N-acetylcysteine; in intermediate form => ECO:0000250\|UniProtKB:P62737

Chain	Residue	Details
B	CYS0
A	GLU209
A	ASP259
A	GLU302
A	ASP303
A	GLU327
D	GLY65
D	ASP66
D	GLU97
D	ASP109
D	GLY114
E	CYS0
D	ALA116
D	VAL145
D	GLY186
D	ASP187
D	GLU209
D	ASP259
D	GLU302
D	ASP303
D	GLU327
A	GLU97
A	ASP109
A	GLY114
A	ALA116
A	VAL145
A	GLY186
A	ASP187

site_id	SWS_FT_FI2
Number of Residues	2
Details	MOD_RES: N-acetylaspartate; in Actin, alpha skeletal muscle => ECO:0000269\|PubMed:1150665

Chain	Residue	Details
B	ASP1
E	ASP1
D	LYS135
D	ARG161

site_id	SWS_FT_FI3
Number of Residues	4
Details	MOD_RES: Methionine (R)-sulfoxide => ECO:0000250\|UniProtKB:P68134

Chain	Residue	Details
B	MET44
B	MET47
E	MET44
E	MET47

site_id	SWS_FT_FI4
Number of Residues	2
Details	MOD_RES: N6-malonyllysine => ECO:0000250

Chain	Residue	Details
B	LYS61
E	LYS61

site_id	SWS_FT_FI5
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
B	HIS73
E	HIS73

site_id	SWS_FT_FI6
Number of Residues	2
Details	MOD_RES: N6-methyllysine => ECO:0000250\|UniProtKB:P68133

Chain	Residue	Details
B	LYS84
E	LYS84

site_id	SWS_FT_FI7
Number of Residues	2
Details	MOD_RES: ADP-ribosylarginine; by SpvB => ECO:0000305\|PubMed:16905096

Chain	Residue	Details
B	ARG177
E	ARG177

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