6D20

Crystal structure of Tyrosine-protein kinase receptor in complex with 5-(4-fluorophenyl)thieno[2,3-d]pyrimidin-4(3H)-one and 5-{[2,4-dichloro-5-(pyridin-2-yl)benzene-1-carbonyl]amino}-N-(2-hydroxy-2-methylpropyl)-1-phenyl-1H-pyrazole-3-carboxamide Inhibitors

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004672	molecular_function	protein kinase activity
A	0004713	molecular_function	protein tyrosine kinase activity
A	0004714	molecular_function	transmembrane receptor protein tyrosine kinase activity
A	0005524	molecular_function	ATP binding
A	0006468	biological_process	protein phosphorylation
A	0007169	biological_process	cell surface receptor protein tyrosine kinase signaling pathway
A	0016020	cellular_component	membrane

Functional Information from PDB Data

site_id	AC1
Number of Residues	9
Details	binding site for residue FQD A 801

Chain	Residue
A	LEU512
A	LYS513
A	TRP514
A	GLU515
A	PHE525
A	PHE525
A	ALA545
A	LYS547
A	HOH999

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site_id	AC2
Number of Residues	15
Details	binding site for residue FQG A 802

Chain	Residue
A	SER484
A	GLY485
A	LEU486
A	LYS544
A	GLU560
A	LEU564
A	VAL573
A	PHE589
A	PHE646
A	HIS648
A	GLY667
A	ASP668
A	GLY670
A	ARG673
A	HOH918

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Functional Information from PROSITE/UniProt

site_id	PS00107
Number of Residues	29
Details	PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGEGAFGKVFlAechnllpeqdkml.....VAVK

Chain	Residue	Details
A	LEU516-LYS544

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

Chain	Residue	Details
A	PHE646-VAL658

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site_id	PS00239
Number of Residues	9
Details	RECEPTOR_TYR_KIN_II Receptor tyrosine kinase class II signature. DIYstdYYR

Chain	Residue	Details
A	ASP674-ARG682

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	15
Details	TRANSMEM: Helical => ECO:0000255

Chain	Residue	Details
A	GLY522-ASP537

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site_id	SWS_FT_FI2
Number of Residues	1
Details	ACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10028

Chain	Residue	Details
A	ARG748

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site_id	SWS_FT_FI3
Number of Residues	2
Details	BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159

Chain	Residue	Details
A	GLY614
A	ALA642

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site_id	SWS_FT_FI4
Number of Residues	1
Details	SITE: Breakpoint for translocation to form TRK and TRK-T3

Chain	Residue	Details
A	TYR496

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site_id	SWS_FT_FI5
Number of Residues	1
Details	SITE: Breakpoint for translocation to form TRK-T1

Chain	Residue	Details
A	PRO584

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site_id	SWS_FT_FI6
Number of Residues	1
Details	SITE: Interaction with SHC1

Chain	Residue	Details
A	HIS594

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site_id	SWS_FT_FI7
Number of Residues	1
Details	MOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:15488758, ECO:0000269|PubMed:27676246, ECO:0000269|PubMed:8155326

Chain	Residue	Details
A	HIS594

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site_id	SWS_FT_FI8
Number of Residues	1
Details	MOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:8155326

Chain	Residue	Details
A	ILE774

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site_id	SWS_FT_FI9
Number of Residues	2
Details	MOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:15488758, ECO:0000269|PubMed:8155326

Chain	Residue	Details
A	HIS778
A	ALA779

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site_id	SWS_FT_FI10
Number of Residues	1
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255

Chain	Residue	Details
A	ASP499

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