7C2H

Crystal Structure of the Thorarchaeota 2DGel3/rabbit actin complex

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
G	0005546	molecular_function	phosphatidylinositol-4,5-bisphosphate binding
G	0005737	cellular_component	cytoplasm
G	0008154	biological_process	actin polymerization or depolymerization
G	0015629	cellular_component	actin cytoskeleton
G	0046872	molecular_function	metal ion binding
G	0051014	biological_process	actin filament severing
G	0051015	molecular_function	actin filament binding
G	0051016	biological_process	barbed-end actin filament capping

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	binding site for residue CA A 401

Chain	Residue
A	ATP402
A	HOH508
A	HOH511
A	HOH529
A	HOH553
A	HOH564

---

site_id	AC2
Number of Residues	26
Details	binding site for residue ATP A 402

Chain	Residue
A	LEU16
A	LYS18
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	CA401
A	HOH511
A	HOH518
A	HOH520
A	HOH529
A	HOH530
A	HOH543
A	HOH550
A	GLY13
A	SER14
A	GLY15

---

site_id	AC3
Number of Residues	6
Details	binding site for residue CA G 301

Chain	Residue
G	GLY26
G	ASP27
G	GLU49
G	ASP95
G	THR96
G	HOH418

---

site_id	AC4
Number of Residues	6
Details	binding site for residue CA G 302

Chain	Residue
A	GLU167
G	ASP61
G	GLY66
G	ALA68
G	HOH435
G	HOH436

---

site_id	AC5
Number of Residues	5
Details	binding site for residue CA G 303

Chain	Residue
A	VAL30
A	HOH512
A	HOH566
G	GLU174
G	HOH422

---

site_id	AC6
Number of Residues	6
Details	binding site for residue CA G 304

Chain	Residue
G	HIS116
G	ASP137
G	ASP138
G	GLU160
G	HOH414
G	HOH437

---

site_id	AC7
Number of Residues	5
Details	binding site for residue CA G 305

Chain	Residue
G	ASP172
G	ARG175
G	GLY177
G	GLN179
G	HOH417

---

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	1
Details	MOD_RES: N-acetylcysteine; in intermediate form => ECO:0000250|UniProtKB:P62737

Chain	Residue	Details
A	CYS0

---

site_id	SWS_FT_FI2
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_FI3
Number of Residues	2
Details	MOD_RES: Methionine (R)-sulfoxide => ECO:0000250|UniProtKB:P68134

Chain	Residue	Details
A	MET44
A	MET47

---

site_id	SWS_FT_FI4
Number of Residues	1
Details	MOD_RES: N6-malonyllysine => ECO:0000250

Chain	Residue	Details
A	LYS61

---

site_id	SWS_FT_FI5
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	HIC73

---

site_id	SWS_FT_FI6
Number of Residues	1
Details	MOD_RES: N6-methyllysine => ECO:0000250|UniProtKB:P68133

Chain	Residue	Details
A	LYS84

---

site_id	SWS_FT_FI7
Number of Residues	1
Details	MOD_RES: ADP-ribosylarginine; by SpvB => ECO:0000305|PubMed:16905096

Chain	Residue	Details
A	ARG177

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