1ESV

COMPLEX BETWEEN LATRUNCULIN A:RABBIT MUSCLE ALPHA ACTIN:HUMAN GELSOLIN DOMAIN 1

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
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	0051015	molecular_function	actin filament binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA A 385

Chain	Residue
A	ATP380
A	HOH1004
A	HOH1007
A	HOH1009
A	HOH1033
A	HOH1065

---

site_id	AC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CA S 390

Chain	Residue
S	GLY90
S	ALA92
A	GLU167
A	HOH1263
S	ASP85

---

site_id	AC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CA S 395

Chain	Residue
S	GLY41
S	ASP42
S	GLU73
S	VAL121
S	HOH1306

---

site_id	AC4
Number of Residues	29
Details	BINDING SITE FOR RESIDUE ATP A 380

Chain	Residue
A	GLY13
A	SER14
A	GLY15
A	LEU16
A	LYS18
A	GLY74
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	CA385
A	LAR401
A	HOH1009
A	HOH1028
A	HOH1039
A	HOH1057
A	HOH1065
A	HOH1071
A	HOH1336

---

site_id	AC5
Number of Residues	14
Details	BINDING SITE FOR RESIDUE LAR A 401

Chain	Residue
A	GLY15
A	LEU16
A	PRO32
A	ILE34
A	GLN59
A	TYR69
A	ASP157
A	GLY182
A	ARG183
A	THR186
A	ARG206
A	ARG210
A	ATP380
A	HOH1342

---

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	82
Details	Repeat: {"description":"Gelsolin-like 1","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	123
Details	Region: {"description":"Actin-severing","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	3
Details	Region: {"description":"Actin-actin interfilament contact point"}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	7
Details	Binding site: {"evidences":[{"source":"PubMed","id":"19666512","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3FFK","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	7
Details	Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI6
Number of Residues	1
Details	Modified residue: {"description":"Phosphotyrosine; by SRC; in vitro","evidences":[{"source":"PubMed","id":"10210201","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI7
Number of Residues	25
Details	Region: {"description":"Interaction with alpha-actinin","evidences":[{"source":"PubMed","id":"8449927","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI8
Number of Residues	1
Details	Modified residue: {"description":"N6-malonyllysine","evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI9
Number of Residues	1
Details	Modified residue: {"description":"Tele-methylhistidine","evidences":[{"source":"PubMed","id":"1150665","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16905096","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"213279","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"2395459","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"499690","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1ATN","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1NWK","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI10
Number of Residues	1
Details	Modified residue: {"description":"N6-methyllysine","evidences":[{"source":"UniProtKB","id":"P68133","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI11
Number of Residues	1
Details	Modified residue: {"description":"ADP-ribosylarginine; by SpvB","evidences":[{"source":"PubMed","id":"16905096","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

---