5WR7

Crystal structure of Trk-A complexed with a selective inhibitor CH7057288

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	25
Details	binding site for residue RCH A 801

Chain	Residue
A	TYR496
A	TYR591
A	MET592
A	ARG593
A	GLY595
A	ASP596
A	LEU611
A	ALA612
A	GLY613
A	PRO619
A	PHE646
A	VAL524
A	LEU657
A	ILE666
A	GLY667
A	ASP668
A	PHE669
A	HOH902
A	ALA542
A	LYS544
A	GLU560
A	LEU564
A	ILE572
A	PHE589
A	GLU590

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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	1
Details	ACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10028

Chain	Residue	Details
A	ASP650

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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	LEU516
A	LYS544

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site_id	SWS_FT_FI3
Number of Residues	1
Details	SITE: Interaction with SHC1

Chain	Residue	Details
A	TYR496

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site_id	SWS_FT_FI4
Number of Residues	1
Details	SITE: Interaction with PLCG1

Chain	Residue	Details
A	TYR791

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site_id	SWS_FT_FI5
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	TYR496

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site_id	SWS_FT_FI6
Number of Residues	1
Details	MOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:8155326

Chain	Residue	Details
A	TYR676

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site_id	SWS_FT_FI7
Number of Residues	2
Details	MOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:15488758, ECO:0000269|PubMed:8155326

Chain	Residue	Details
A	TYR680
A	TYR681

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site_id	SWS_FT_FI8
Number of Residues	1
Details	MOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:15488758, ECO:0000269|PubMed:7510697, ECO:0000269|PubMed:8155326

Chain	Residue	Details
A	TYR791

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