7UDU

cryo-EM structure of the ADP state wild type myosin-15-F-actin complex (symmetry expansion and re-centering)

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0001725	cellular_component	stress fiber
A	0005515	molecular_function	protein 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	0016787	molecular_function	hydrolase activity
A	0030240	biological_process	skeletal muscle thin filament assembly
A	0048741	biological_process	skeletal muscle fiber development
B	0001725	cellular_component	stress fiber
B	0005515	molecular_function	protein binding
B	0005524	molecular_function	ATP binding
B	0005737	cellular_component	cytoplasm
B	0005856	cellular_component	cytoskeleton
B	0005865	cellular_component	striated muscle thin filament
B	0005884	cellular_component	actin filament
B	0016787	molecular_function	hydrolase activity
B	0030240	biological_process	skeletal muscle thin filament assembly
B	0048741	biological_process	skeletal muscle fiber development
C	0001725	cellular_component	stress fiber
C	0005515	molecular_function	protein binding
C	0005524	molecular_function	ATP binding
C	0005737	cellular_component	cytoplasm
C	0005856	cellular_component	cytoskeleton
C	0005865	cellular_component	striated muscle thin filament
C	0005884	cellular_component	actin filament
C	0016787	molecular_function	hydrolase activity
C	0030240	biological_process	skeletal muscle thin filament assembly
C	0048741	biological_process	skeletal muscle fiber development
D	0003774	molecular_function	cytoskeletal motor activity
D	0005524	molecular_function	ATP binding
D	0016459	cellular_component	myosin complex
E	0005509	molecular_function	calcium ion binding

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

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

Chain	Residue	Details
E	ASP42-LEU54

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00448

Chain	Residue	Details
C	MET44
C	MET47
E	ASP42
E	ASN44
E	ASP46
E	ASP53

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site_id	SWS_FT_FI2
Number of Residues	3
Details	MOD_RES: Tele-methylhistidine => ECO:0000269|PubMed:12356759, ECO:0007744|PDB:1MDU

Chain	Residue	Details
A	HIC73
B	HIC73
C	HIC73

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site_id	SWS_FT_FI3
Number of Residues	3
Details	MOD_RES: N6-methyllysine => ECO:0000250|UniProtKB:P68133

Chain	Residue	Details
A	LYS84
B	LYS84
C	LYS84

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