4UY9

Structure of MLK1 kinase domain with leucine zipper 1

Functional Information from GO Data

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

Functional Information from PROSITE/UniProt

site_id	PS00107
Number of Residues	22
Details	PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. IGIGGFGKVYrAfwigde............VAVK

Chain	Residue	Details
A	ILE150-LYS171

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

Chain	Residue	Details
A	ILE264-ILE276

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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	ASP268
B	ASP268

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site_id	SWS_FT_FI2
Number of Residues	2
Details	BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159

Chain	Residue	Details
A	ILE150
B	ILE150

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site_id	SWS_FT_FI3
Number of Residues	2
Details	BINDING:

Chain	Residue	Details
A	LYS171
B	LYS171

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site_id	SWS_FT_FI4
Number of Residues	6
Details	MOD_RES: Phosphothreonine; by autocatalysis => ECO:0000269|PubMed:15610029

Chain	Residue	Details
A	THR304
A	THR305
A	THR312
B	THR304
B	THR305
B	THR312

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site_id	SWS_FT_FI5
Number of Residues	2
Details	MOD_RES: Phosphoserine; by autocatalysis => ECO:0000269|PubMed:15610029

Chain	Residue	Details
A	SER308
B	SER308

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