4JXF

Crystal Structure of PLK4 Kinase with an inhibitor: 400631 ((1R,2S)-2-{3-[(E)-2-{4-[(DIMETHYLAMINO)METHYL]PHENYL}ETHENYL]-2H-INDAZOL-6-YL}-5'-METHOXYSPIRO[CYCLOPROPANE-1,3'-INDOL]-2'(1'H)-ONE)

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

Functional Information from PDB Data

site_id	AC1
Number of Residues	16
Details	BINDING SITE FOR RESIDUE 631 A 301

Chain	Residue
A	LEU18
A	HIS93
A	SER140
A	LEU142
A	LEU143
A	ALA153
A	THR159
A	GLN160
A	GLY19
A	PHE23
A	VAL26
A	ALA39
A	LYS41
A	GLU90
A	MET91
A	CYS92

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site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE EDO A 302

Chain	Residue
A	ARG135
A	SER140
A	ASP154
A	HOH410

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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. LGKGSFAGVYrAesihtgle..........VAIK

Chain	Residue	Details
A	LEU18-LYS41

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site_id	PS00109
Number of Residues	13
Details	PROTEIN_KINASE_TYR Tyrosine protein kinases specific active-site signature. ILHrDLTLSNLLL

Chain	Residue	Details
A	ILE132-LEU144

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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

Chain	Residue	Details
A	ASP136

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site_id	SWS_FT_FI2
Number of Residues	1
Details	BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159

Chain	Residue	Details
A	LEU18

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site_id	SWS_FT_FI3
Number of Residues	1
Details	BINDING: BINDING => ECO:0000305

Chain	Residue	Details
A	LYS41

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site_id	SWS_FT_FI4
Number of Residues	2
Details	MOD_RES: N6-acetyllysine => ECO:0000269|PubMed:27796307

Chain	Residue	Details
A	LYS45
A	LYS46

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