3MN5

Structures of actin-bound WH2 domains of Spire and the implication for filament nucleation

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
S	0003779	molecular_function	actin binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CA A 901

Chain	Residue
A	HOH450
A	HOH479
A	HOH787
A	ATP800

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site_id	AC2
Number of Residues	30
Details	BINDING SITE FOR RESIDUE ATP A 800

Chain	Residue
A	GLY156
A	ASP157
A	GLY158
A	VAL159
A	GLY182
A	ARG210
A	LYS213
A	GLU214
A	GLY301
A	GLY302
A	THR303
A	MET305
A	TYR306
A	LYS336
A	HOH414
A	HOH450
A	HOH479
A	HOH480
A	HOH515
A	HOH524
A	HOH585
A	HOH624
A	HOH726
A	HOH787
A	CA901
A	GLY13
A	SER14
A	GLY15
A	LEU16
A	LYS18

---

site_id	AC3
Number of Residues	11
Details	BINDING SITE FOR RESIDUE LAB A 376

Chain	Residue
A	GLY15
A	LEU16
A	HOH42
A	TYR69
A	ASP157
A	ARG183
A	THR186
A	ARG206
A	GLU207
A	ARG210
A	LYS213

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Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	TRP356-GLU364

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

Chain	Residue	Details
A	LEU104-ARG116

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	MOD_RES: N-acetylaspartate; in Actin, alpha skeletal muscle => ECO:0000269|PubMed:1150665

Chain	Residue	Details
A	ASP1

---

site_id	SWS_FT_FI2
Number of Residues	2
Details	MOD_RES: Methionine (R)-sulfoxide => ECO:0000250|UniProtKB:P68134

Chain	Residue	Details
A	SER63
A	GLY65

---

site_id	SWS_FT_FI3
Number of Residues	1
Details	MOD_RES: N6-malonyllysine => ECO:0000250

Chain	Residue	Details
A	THR77

---

site_id	SWS_FT_FI4
Number of Residues	1
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	THR89

---

site_id	SWS_FT_FI5
Number of Residues	1
Details	MOD_RES: N6-methyllysine => ECO:0000250|UniProtKB:P68133

Chain	Residue	Details
A	GLU100

---

site_id	SWS_FT_FI6
Number of Residues	1
Details	MOD_RES: ADP-ribosylarginine; by SpvB => ECO:0000305|PubMed:16905096

Chain	Residue	Details
A	LEU193

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