3L8P

Crystal structure of cytoplasmic kinase domain of Tie2 complexed with inhibitor CEP11207

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	0005524	molecular_function	ATP binding
A	0006468	biological_process	protein phosphorylation

Functional Information from PDB Data

site_id	AC1
Number of Residues	14
Details	BINDING SITE FOR RESIDUE 0CE A 2207

Chain	Residue
A	ILE830
A	GLY908
A	ARG968
A	LEU971
A	ASP982
A	PHE983
A	GLY831
A	GLU832
A	VAL838
A	ALA853
A	ILE902
A	GLU903
A	TYR904
A	ALA905

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Functional Information from PROSITE/UniProt

site_id	PS00107
Number of Residues	26
Details	PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. IGEGNFGQVLkArikkdglrmd........AAIK

Chain	Residue	Details
A	ILE830-LYS855

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

Chain	Residue	Details
A	PHE960-VAL972

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	ACT_SITE: Proton acceptor => ECO:0000305|PubMed:11080633

Chain	Residue	Details
A	ASP964

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site_id	SWS_FT_FI2
Number of Residues	2
Details	BINDING: BINDING => ECO:0000305

Chain	Residue	Details
A	ILE830
A	LYS855

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site_id	SWS_FT_FI3
Number of Residues	3
Details	MOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:11513602

Chain	Residue	Details
A	TYR860
A	TYR992
A	TYR1108

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site_id	SWS_FT_FI4
Number of Residues	1
Details	MOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:14665640, ECO:0000269|PubMed:27270174

Chain	Residue	Details
A	TYR1102

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