5SAU

DDR1, 3-[2-(6-aminopyridin-3-yl)ethynyl]-N-[3-(trifluoromethyl)phenyl]benzamide, 1.800A, P212121, Rfree=23.1%

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 PROSITE/UniProt

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

Chain	Residue	Details
A	PHE756-VAL768

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

Chain	Residue	Details
A	ASN784-ARG792

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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	CYS766

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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	LEU616

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site_id	SWS_FT_FI3
Number of Residues	1
Details	BINDING:

Chain	Residue	Details
A	LYS655

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site_id	SWS_FT_FI4
Number of Residues	1
Details	MOD_RES: Phosphoserine => ECO:0007744|PubMed:19369195

Chain	Residue	Details
A	SER631

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site_id	SWS_FT_FI5
Number of Residues	1
Details	MOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000305|PubMed:16337946

Chain	Residue	Details
A	VAL740

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site_id	SWS_FT_FI6
Number of Residues	3
Details	MOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:24509848

Chain	Residue	Details
A	ARG792
A	ARG796
A	ALA797

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