1NR0

Two Seven-Bladed Beta-Propeller Domains Revealed By The Structure Of A C. elegans Homologue Of Yeast Actin Interacting Protein 1 (AIP1).

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003779	molecular_function	actin binding
A	0005737	cellular_component	cytoplasm
A	0005856	cellular_component	cytoskeleton
A	0007015	biological_process	actin filament organization
A	0016528	cellular_component	sarcoplasm
A	0030016	cellular_component	myofibril
A	0030042	biological_process	actin filament depolymerization
A	0030240	biological_process	skeletal muscle thin filament assembly
A	0030833	biological_process	regulation of actin filament polymerization
A	0030834	biological_process	regulation of actin filament depolymerization
A	0030836	biological_process	positive regulation of actin filament depolymerization
A	0030837	biological_process	negative regulation of actin filament polymerization
A	0030864	cellular_component	cortical actin cytoskeleton
A	0040011	biological_process	locomotion
A	0040012	biological_process	regulation of locomotion
A	0045214	biological_process	sarcomere organization
A	0051015	molecular_function	actin filament binding
A	0071689	biological_process	muscle thin filament assembly

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MN A 700

Chain	Residue
A	ASP154
A	HOH839
A	HOH864
A	HOH1016
A	HOH1159
A	HOH1411

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Functional Information from PROSITE/UniProt

site_id	PS00678
Number of Residues	15
Details	WD_REPEATS_1 Trp-Asp (WD) repeats signature. IASAsaDkTIKIWNV

Chain	Residue	Details
A	ILE254-VAL268
A	LEU551-MET565
A	ILE595-VAL609

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