2Y3A

Crystal structure of p110beta in complex with icSH2 of p85beta and the drug GDC-0941

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
A	0001935	biological_process	endothelial cell proliferation
A	0001952	biological_process	regulation of cell-matrix adhesion
A	0002931	biological_process	response to ischemia
A	0003376	biological_process	sphingosine-1-phosphate receptor signaling pathway
A	0004674	molecular_function	protein serine/threonine kinase activity
A	0005515	molecular_function	protein binding
A	0005524	molecular_function	ATP binding
A	0005634	cellular_component	nucleus
A	0005654	cellular_component	nucleoplasm
A	0005730	cellular_component	nucleolus
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0005886	cellular_component	plasma membrane
A	0005942	cellular_component	phosphatidylinositol 3-kinase complex
A	0005943	cellular_component	phosphatidylinositol 3-kinase complex, class IA
A	0006629	biological_process	lipid metabolic process
A	0006874	biological_process	intracellular calcium ion homeostasis
A	0006897	biological_process	endocytosis
A	0006914	biological_process	autophagy
A	0007155	biological_process	cell adhesion
A	0007156	biological_process	homophilic cell-cell adhesion
A	0010595	biological_process	positive regulation of endothelial cell migration
A	0010628	biological_process	positive regulation of gene expression
A	0016301	molecular_function	kinase activity
A	0016303	molecular_function	1-phosphatidylinositol-3-kinase activity
A	0016477	biological_process	cell migration
A	0016740	molecular_function	transferase activity
A	0030168	biological_process	platelet activation
A	0030496	cellular_component	midbody
A	0031526	cellular_component	brush border membrane
A	0033031	biological_process	positive regulation of neutrophil apoptotic process
A	0035005	molecular_function	1-phosphatidylinositol-4-phosphate 3-kinase activity
A	0035022	biological_process	positive regulation of Rac protein signal transduction
A	0036092	biological_process	phosphatidylinositol-3-phosphate biosynthetic process
A	0040016	biological_process	embryonic cleavage
A	0042267	biological_process	natural killer cell mediated cytotoxicity
A	0043409	biological_process	negative regulation of MAPK cascade
A	0043491	biological_process	phosphatidylinositol 3-kinase/protein kinase B signal transduction
A	0043560	molecular_function	insulin receptor substrate binding
A	0045429	biological_process	positive regulation of nitric oxide biosynthetic process
A	0046854	biological_process	phosphatidylinositol phosphate biosynthetic process
A	0046934	molecular_function	1-phosphatidylinositol-4,5-bisphosphate 3-kinase activity
A	0048015	biological_process	phosphatidylinositol-mediated signaling
A	0051898	biological_process	negative regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction
A	0060055	biological_process	angiogenesis involved in wound healing
A	0106310	molecular_function	protein serine kinase activity
A	1900747	biological_process	negative regulation of vascular endothelial growth factor signaling pathway
A	1903298	biological_process	negative regulation of hypoxia-induced intrinsic apoptotic signaling pathway
A	1903671	biological_process	negative regulation of sprouting angiogenesis

Functional Information from PDB Data

site_id	AC1
Number of Residues	12
Details	BINDING SITE FOR RESIDUE GD9 A 2058

Chain	Residue
A	TYR772
A	MET920
A	ILE930
A	ASP931
A	MET773
A	ASP774
A	ASP807
A	TYR833
A	ILE845
A	GLU846
A	VAL847
A	VAL848

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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. FKng.DDLRQDmltlQ

Chain	Residue	Details
A	PHE798-GLN812

---

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

Chain	Residue	Details
A	SER898-ASN918

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	89
Details	Domain: {"description":"PI3K-ABD","evidences":[{"source":"PROSITE-ProRule","id":"PRU00877","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	281
Details	Domain: {"description":"PI3K/PI4K catalytic","evidences":[{"source":"PROSITE-ProRule","id":"PRU00269","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	6
Details	Region: {"description":"G-loop","evidences":[{"source":"PROSITE-ProRule","id":"PRU00269","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	8
Details	Region: {"description":"Catalytic loop","evidences":[{"source":"PROSITE-ProRule","id":"PRU00269","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	26
Details	Region: {"description":"Activation loop","evidences":[{"source":"PROSITE-ProRule","id":"PRU00269","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI6
Number of Residues	94
Details	Domain: {"description":"SH2 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00191","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI7
Number of Residues	1
Details	Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"15592455","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"17947660","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"18034455","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI8
Number of Residues	1
Details	Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"O00459","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

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