3MYH

Insights into the Importance of Hydrogen Bonding in the Gamma-Phosphate Binding Pocket of Myosin: Structural and Functional Studies of Ser236

Functional Information from GO Data

Chain	GOid	namespace	contents
X	0003774	molecular_function	cytoskeletal motor activity
X	0005524	molecular_function	ATP binding
X	0016459	cellular_component	myosin complex
X	0051015	molecular_function	actin filament binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG X 997

Chain	Residue
X	THR186
X	SER237
X	HOH780
X	HOH787
X	VO4998
X	ADP999

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site_id	AC2
Number of Residues	12
Details	BINDING SITE FOR RESIDUE VO4 X 998

Chain	Residue
X	ASN233
X	ALA236
X	SER237
X	GLY457
X	HOH780
X	HOH787
X	HOH792
X	MG997
X	ADP999
X	SER181
X	GLY182
X	LYS185

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site_id	AC3
Number of Residues	21
Details	BINDING SITE FOR RESIDUE ADP X 999

Chain	Residue
X	ASN127
X	PRO128
X	PHE129
X	LYS130
X	TYR135
X	GLY182
X	ALA183
X	GLY184
X	LYS185
X	THR186
X	GLU187
X	ASN233
X	HOH774
X	HOH777
X	HOH780
X	HOH787
X	HOH908
X	MG997
X	VO4998
X	HOH1016
X	HOH1049

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site_id	AC4
Number of Residues	11
Details	BINDING SITE FOR RESIDUE BIT X 800

Chain	Residue
X	ARG238
X	PHE239
X	GLY240
X	TYR261
X	LEU262
X	SER456
X	GLU467
X	CYS470
X	TYR634
X	LEU641
X	HOH927

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	52
Details	Domain: {"description":"Myosin N-terminal SH3-like","evidences":[{"source":"PROSITE-ProRule","id":"PRU01190","evidenceCode":"ECO:0000255"}]}

Chain

Residue

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site_id	SWS_FT_FI2
Number of Residues	22
Details	Region: {"description":"Actin-binding"}

Chain

Residue

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site_id	SWS_FT_FI3
Number of Residues	7
Details	Binding site: {}

Chain

Residue

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site_id	SWS_FT_FI4
Number of Residues	1
Details	Modified residue: {"description":"N6,N6-dimethyllysine","evidences":[{"evidenceCode":"ECO:0000255"}]}

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Catalytic Information from CSA

site_id	MCSA1
Number of Residues	8
Details	M-CSA 534

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