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5JHA

Structure of Phosphoinositide 3-kinase gamma (PI3K) bound to the potent inhibitor PIKin2

Functional Information from GO Data
ChainGOidnamespacecontents
A0016301molecular_functionkinase activity
A0046854biological_processphosphatidylinositol phosphate biosynthetic process
Functional Information from PDB Data
site_idAC1
Number of Residues14
Detailsbinding site for residue 6K7 A 1201
ChainResidue
AMET804
AVAL882
AMET953
AILE963
AASP964
AHOH1321
AILE831
ALYS833
AASP836
ALEU838
AASP841
AILE879
AGLU880
AILE881

site_idAC2
Number of Residues4
Detailsbinding site for residue SO4 A 1202
ChainResidue
AALA545
ATRP576
AARG579
AHOH1346

site_idAC3
Number of Residues4
Detailsbinding site for residue SO4 A 1203
ChainResidue
APRO206
ALEU207
ATRP212
ALYS288

site_idAC4
Number of Residues6
Detailsbinding site for residue SO4 A 1204
ChainResidue
AHIS199
ALYS689
AARG690
AHIS693
AARG784
APRO789

site_idAC5
Number of Residues5
Detailsbinding site for residue SO4 A 1205
ChainResidue
ALEU657
APHE694
APHE698
AGLN846
AHOH1347

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 Residues3
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
AGLY829
ALEU864
APHE961

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: Phosphothreonine; by PKA => ECO:0000250|UniProtKB:Q9JHG7
ChainResidueDetails
ATHR1024

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: Phosphoserine; by autocatalysis => ECO:0000269|PubMed:12502714
ChainResidueDetails
ASER1101

218853

PDB entries from 2024-04-24

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