4G11

X-ray structure of PI3K-gamma bound to a 4-(morpholin-4-yl)- (6-oxo-1,6-dihydropyrimidin-2-yl)amide inhibitor

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0016301	molecular_function	kinase activity
A	0046854	biological_process	phosphatidylinositol phosphate biosynthetic process

Functional Information from PDB Data

site_id	AC1
Number of Residues	10
Details	BINDING SITE FOR RESIDUE 0W7 A 1201

Chain	Residue
A	MET804
A	ASP964
A	PRO810
A	TRP812
A	LYS833
A	GLU880
A	ILE881
A	VAL882
A	MET953
A	ILE963

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Functional Information from PROSITE/UniProt

site_id	PS00915
Number of Residues	15
Details	PI3_4_KINASE_1 Phosphatidylinositol 3- and 4-kinases signature 1. FKhg.DDLRQDmlilQ

Chain	Residue	Details
A	PHE832-GLN846

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site_id	PS00916
Number of Residues	21
Details	PI3_4_KINASE_2 Phosphatidylinositol 3- and 4-kinases signature 2. ScAgycVatFVLgIgDRHndN

Chain	Residue	Details
A	SER931-ASN951

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	3
Details	BINDING: BINDING => ECO:0000250

Chain	Residue	Details
A	GLY829
A	LEU864
A	PHE961

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site_id	SWS_FT_FI2
Number of Residues	1
Details	MOD_RES: Phosphothreonine; by PKA => ECO:0000250|UniProtKB:Q9JHG7

Chain	Residue	Details
A	THR1024

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site_id	SWS_FT_FI3
Number of Residues	1
Details	MOD_RES: Phosphoserine; by autocatalysis => ECO:0000269|PubMed:12502714

Chain	Residue	Details
A	SER1101

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