4UMR

Structure of MELK in complex with inhibitors

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

Functional Information from PDB Data

site_id	AC1
Number of Residues	10
Details	BINDING SITE FOR RESIDUE QBB A 1334

Chain	Residue
A	ILE17
A	ILE149
A	VAL25
A	LEU27
A	ALA38
A	LYS40
A	GLU87
A	TYR88
A	CYS89
A	LEU139

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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	1
Details	ACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027

Chain	Residue	Details
A	ASP132

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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	ILE17
A	LYS40

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site_id	SWS_FT_FI3
Number of Residues	1
Details	MOD_RES: Phosphothreonine; by autocatalysis => ECO:0000269|PubMed:16216881

Chain	Residue	Details
A	THR56

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site_id	SWS_FT_FI4
Number of Residues	1
Details	MOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:16216881

Chain	Residue	Details
A	TYR163

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site_id	SWS_FT_FI5
Number of Residues	1
Details	MOD_RES: Phosphothreonine; by autocatalysis => ECO:0000269|PubMed:14976552, ECO:0000269|PubMed:16216881, ECO:0000269|PubMed:16628004

Chain	Residue	Details
A	ALA167

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site_id	SWS_FT_FI6
Number of Residues	3
Details	MOD_RES: Phosphoserine; by autocatalysis => ECO:0000269|PubMed:16216881

Chain	Residue	Details
A	SER171
A	SER253
A	SER336

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