6YLL

Biochemical, Cellular and Structural Characterization of Novel ERK3 Inhibitors

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004672	molecular_function	protein kinase activity
A	0004707	molecular_function	MAP kinase activity
A	0005524	molecular_function	ATP binding
A	0006468	biological_process	protein phosphorylation
B	0004672	molecular_function	protein kinase activity
B	0004707	molecular_function	MAP kinase activity
B	0005524	molecular_function	ATP binding
B	0006468	biological_process	protein phosphorylation

Functional Information from PDB Data

site_id	AC1
Number of Residues	8
Details	binding site for residue OYB A 401

Chain	Residue
A	VAL34
A	GLN108
A	GLU109
A	TYR110
A	MET111
A	GLU112
A	PHE159
B	GLU163

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Functional Information from PROSITE/UniProt

site_id	PS00107
Number of Residues	25
Details	PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGCGGNGLVFsAvdndcdkrv.........AIKK

Chain	Residue	Details
A	LEU26-LYS50

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site_id	PS00108
Number of Residues	13
Details	PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. VlHrDLKpaNLFI

Chain	Residue	Details
A	VAL148-ILE160

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	ACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027

Chain	Residue	Details
A	ASP152
B	ASP152

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site_id	SWS_FT_FI2
Number of Residues	4
Details	BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159

Chain	Residue	Details
A	LEU26
A	LYS49
B	LEU26
B	LYS49

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site_id	SWS_FT_FI3
Number of Residues	2
Details	MOD_RES: Phosphoserine; by PAK1, PAK2 and PAK3 => ECO:0000269|PubMed:21177870, ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:23186163

Chain	Residue	Details
A	SER189
B	SER189

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