5H53

The structure of rabbit skeletal muscle actomyosin rigor complex at 5.2 angstrom.

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003774	molecular_function	cytoskeletal motor activity
A	0005524	molecular_function	ATP binding
A	0016459	cellular_component	myosin complex
A	0051015	molecular_function	actin filament binding
B	0005509	molecular_function	calcium ion binding
C	0005509	molecular_function	calcium ion binding
D	0000287	molecular_function	magnesium ion binding
D	0001725	cellular_component	stress fiber
D	0003785	molecular_function	actin monomer binding
D	0005509	molecular_function	calcium ion binding
D	0005515	molecular_function	protein binding
D	0005523	molecular_function	tropomyosin binding
D	0005524	molecular_function	ATP binding
D	0005737	cellular_component	cytoplasm
D	0005856	cellular_component	cytoskeleton
D	0005865	cellular_component	striated muscle thin filament
D	0005884	cellular_component	actin filament
D	0010628	biological_process	positive regulation of gene expression
D	0016787	molecular_function	hydrolase activity
D	0019904	molecular_function	protein domain specific binding
D	0030027	cellular_component	lamellipodium
D	0030041	biological_process	actin filament polymerization
D	0030175	cellular_component	filopodium
D	0030240	biological_process	skeletal muscle thin filament assembly
D	0031013	molecular_function	troponin I binding
D	0031432	molecular_function	titin binding
D	0031941	cellular_component	filamentous actin
D	0032036	molecular_function	myosin heavy chain binding
D	0032432	cellular_component	actin filament bundle
D	0042802	molecular_function	identical protein binding
D	0044297	cellular_component	cell body
D	0048306	molecular_function	calcium-dependent protein binding
D	0048741	biological_process	skeletal muscle fiber development
D	0051017	biological_process	actin filament bundle assembly
D	0090131	biological_process	mesenchyme migration
D	0098723	cellular_component	skeletal muscle myofibril
D	0140660	molecular_function	cytoskeletal motor activator activity
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	12
Details	binding site for residue ADP D 401

Chain	Residue
D	SER14
D	MET305
D	TYR306
D	LYS336
D	GLY156
D	ASP157
D	GLY182
D	LYS213
D	GLU214
D	GLY301
D	GLY302
D	THR303

---

site_id	AC2
Number of Residues	11
Details	binding site for residue ADP E 401

Chain	Residue
E	GLY156
E	ASP157
E	GLY158
E	LYS213
E	GLU214
E	GLY301
E	GLY302
E	THR303
E	MET305
E	TYR306
E	LYS336

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Functional Information from PROSITE/UniProt

site_id	PS00018
Number of Residues	13
Details	EF_HAND_1 EF-hand calcium-binding domain. DQNRDGIIDkeDL

Chain	Residue	Details
B	ASP39-LEU51

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

Chain	Residue	Details
D	TYR53-GLY63

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

Chain	Residue	Details
D	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
D	LEU104-ARG116

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	MOD_RES: N-acetylaspartate; in Actin, alpha skeletal muscle => ECO:0000269|PubMed:1150665

Chain	Residue	Details
D	ASP1
E	ASP1
B	ASP43
B	ASP50

---

site_id	SWS_FT_FI2
Number of Residues	4
Details	MOD_RES: Methionine (R)-sulfoxide => ECO:0000250|UniProtKB:P68134

Chain	Residue	Details
D	MET44
D	MET47
E	MET44
E	MET47

---

site_id	SWS_FT_FI3
Number of Residues	2
Details	MOD_RES: N6-malonyllysine => ECO:0000250

Chain	Residue	Details
D	LYS61
E	LYS61

---

site_id	SWS_FT_FI4
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
D	HIC73
E	HIC73

---

site_id	SWS_FT_FI5
Number of Residues	2
Details	MOD_RES: N6-methyllysine => ECO:0000250|UniProtKB:P68133

Chain	Residue	Details
D	LYS84
E	LYS84

---

site_id	SWS_FT_FI6
Number of Residues	2
Details	MOD_RES: ADP-ribosylarginine; by SpvB => ECO:0000305|PubMed:16905096

Chain	Residue	Details
D	ARG177
E	ARG177

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