6XRL

Crystal structure of human PI3K-gamma in complex with inhibitor IPI-549

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	14
Details	binding site for residue V7Y A 1101

Chain	Residue
A	LYS802
A	VAL882
A	THR887
A	LYS890
A	MET953
A	ILE963
A	MET804
A	PRO810
A	LEU811
A	TRP812
A	TYR867
A	ILE879
A	GLU880
A	ILE881

---

site_id	AC2
Number of Residues	4
Details	binding site for residue SO4 A 1102

Chain	Residue
A	ALA545
A	GLU546
A	TRP576
A	ARG579

---

site_id	AC3
Number of Residues	4
Details	binding site for residue SO4 A 1103

Chain	Residue
A	LEU657
A	PHE694
A	GLN846
A	ARG849

---

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

---

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

---

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

---

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

---

site_id	SWS_FT_FI3
Number of Residues	25
Details	Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

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

---