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3IBE

Crystal Structure of a Pyrazolopyrimidine Inhibitor Bound to PI3 Kinase Gamma

Functional Information from GO Data
ChainGOidnamespacecontents
A0016301molecular_functionkinase activity
A0046854biological_processphosphatidylinositol phosphate biosynthetic process
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 1
ChainResidue
APRO206
ALEU207
ATRP212
ALYS288

site_idAC2
Number of Residues18
DetailsBINDING SITE FOR RESIDUE L64 A 1109
ChainResidue
AASP836
AASP837
ALEU838
AGLN840
AASP841
AILE879
AGLU880
AILE881
AVAL882
AASP950
AMET953
AASP964
AGLY966
AMET804
AALA805
ASER806
AILE831
ALYS833

Functional Information from PROSITE/UniProt
site_idPS00915
Number of Residues15
DetailsPI3_4_KINASE_1 Phosphatidylinositol 3- and 4-kinases signature 1. FKhg.DDLRQDmlilQ
ChainResidueDetails
APHE832-GLN846

site_idPS00916
Number of Residues21
DetailsPI3_4_KINASE_2 Phosphatidylinositol 3- and 4-kinases signature 2. ScAgycVatFVLgIgDRHndN
ChainResidueDetails
ASER931-ASN951

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues182
DetailsDomain: {"description":"PIK helical","evidences":[{"source":"PROSITE-ProRule","id":"PRU00878","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues6
DetailsRegion: {"description":"G-loop","evidences":[{"source":"PROSITE-ProRule","id":"PRU00269","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues8
DetailsRegion: {"description":"Catalytic loop","evidences":[{"source":"PROSITE-ProRule","id":"PRU00269","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues17
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine; by PKA","evidences":[{"source":"UniProtKB","id":"Q9JHG7","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

240971

PDB entries from 2025-08-27

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