4PMS

The structure of TrkA kinase bound to the inhibitor 4-naphthalen-1-yl-1-[(5-phenyl-1,2,4-oxadiazol-3-yl)methyl]-1H-pyrrolo[3,2-c]pyridine-2-carboxylic acid

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	10
Details	binding site for residue 31X A 801

Chain	Residue
A	VAL524
A	MET671
A	ALA542
A	LYS544
A	VAL573
A	PHE589
A	LEU657
A	ASP668
A	PHE669
A	GLY670

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site_id	AC2
Number of Residues	2
Details	binding site for residue CL A 802

Chain	Residue
A	PRO754
A	TYR757

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site_id	AC3
Number of Residues	4
Details	binding site for residue ACT A 803

Chain	Residue
A	GLY625
A	ARG649
A	ARG702
A	HOH903

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site_id	AC4
Number of Residues	4
Details	binding site for residue ACT A 804

Chain	Residue
A	ARG602
A	LYS725
A	GLN726
A	TYR729

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site_id	AC5
Number of Residues	6
Details	binding site for residue ACT A 805

Chain	Residue
A	TRP718
A	THR722
A	LYS725
A	TYR729
A	PRO749
A	HOH917

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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	LYS544
A	LEU516

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site_id	SWS_FT_FI3
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_FI4
Number of Residues	2
Details	MOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:15488758, ECO:0000269|PubMed:8155326

Chain	Residue	Details
A	TYR681
A	TYR680

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