5TX3

Structure of Maternal Embryonic Leucine Zipper Kinase

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004672	molecular_function	protein kinase activity
A	0004674	molecular_function	protein serine/threonine kinase activity
A	0005524	molecular_function	ATP binding
A	0006468	biological_process	protein phosphorylation
B	0004672	molecular_function	protein kinase activity
B	0004674	molecular_function	protein serine/threonine 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	11
Details	binding site for residue 7MY A 1000

Chain	Residue
A	VAL25
A	ILE149
B	THR16
A	LYS40
A	LEU86
A	GLU87
A	TYR88
A	CYS89
A	GLU93
A	GLU136
A	LEU139

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site_id	AC2
Number of Residues	12
Details	binding site for residue 7MY B 1001

Chain	Residue
A	GLU15
A	THR16
B	ILE17
B	VAL25
B	LYS40
B	GLU87
B	TYR88
B	CYS89
B	GLY92
B	GLU93
B	GLU136
B	ILE149

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Functional Information from PROSITE/UniProt

site_id	PS00107
Number of Residues	24
Details	PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. IGTGGFAKVKlAchiltgem..........VAIK

Chain	Residue	Details
A	ILE17-LYS40

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

Chain	Residue	Details
A	TYR128-PHE140

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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	ASP132
B	ASP132

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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	ILE17
A	LYS40
B	ILE17
B	LYS40

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site_id	SWS_FT_FI3
Number of Residues	2
Details	MOD_RES: Phosphothreonine; by autocatalysis => ECO:0000269|PubMed:16216881

Chain	Residue	Details
A	THR56
B	THR56

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site_id	SWS_FT_FI4
Number of Residues	2
Details	MOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:16216881

Chain	Residue	Details
A	TYR163
B	TYR163

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site_id	SWS_FT_FI5
Number of Residues	2
Details	MOD_RES: Phosphothreonine; by autocatalysis => ECO:0000269|PubMed:14976552, ECO:0000269|PubMed:16216881, ECO:0000269|PubMed:16628004

Chain	Residue	Details
A	THR167
B	THR167

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site_id	SWS_FT_FI6
Number of Residues	6
Details	MOD_RES: Phosphoserine; by autocatalysis => ECO:0000269|PubMed:16216881

Chain	Residue	Details
A	SER171
A	SER253
A	SER336
B	SER171
B	SER253
B	SER336

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