2A4Z

Crystal Structure of human PI3Kgamma complexed with AS604850

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	12
Details	BINDING SITE FOR RESIDUE BYM A 101

Chain	Residue
A	PRO810
A	MET953
A	ILE963
A	ASP964
A	TRP812
A	LYS833
A	TYR867
A	ILE879
A	GLU880
A	ILE881
A	VAL882
A	ALA885

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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	6
Details	Region: {"description":"G-loop","evidences":[{"source":"PROSITE-ProRule","id":"PRU00269","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	8
Details	Region: {"description":"Catalytic loop","evidences":[{"source":"PROSITE-ProRule","id":"PRU00269","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI3
Number of Residues	17
Details	Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI4
Number of Residues	1
Details	Modified residue: {"description":"Phosphothreonine; by PKA","evidences":[{"source":"UniProtKB","id":"Q9JHG7","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

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