Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

5NCZ

mPI3Kd IN COMPLEX WITH inh1

Functional Information from GO Data
ChainGOidnamespacecontents
A0001782biological_processB cell homeostasis
A0002250biological_processadaptive immune response
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0005886cellular_componentplasma membrane
A0005942cellular_componentphosphatidylinositol 3-kinase complex
A0006629biological_processlipid metabolic process
A0006935biological_processchemotaxis
A0006954biological_processinflammatory response
A0007166biological_processcell surface receptor signaling pathway
A0010628biological_processpositive regulation of gene expression
A0010629biological_processnegative regulation of gene expression
A0016301molecular_functionkinase activity
A0016303molecular_function1-phosphatidylinositol-3-kinase activity
A0030154biological_processcell differentiation
A0035005molecular_function1-phosphatidylinositol-4-phosphate 3-kinase activity
A0036092biological_processphosphatidylinositol-3-phosphate biosynthetic process
A0042113biological_processB cell activation
A0043491biological_processphosphatidylinositol 3-kinase/protein kinase B signal transduction
A0045087biological_processinnate immune response
A0045766biological_processpositive regulation of angiogenesis
A0046854biological_processphosphatidylinositol phosphate biosynthetic process
A0046934molecular_function1-phosphatidylinositol-4,5-bisphosphate 3-kinase activity
A0048015biological_processphosphatidylinositol-mediated signaling
A0048872biological_processhomeostasis of number of cells
A0050832biological_processdefense response to fungus
Functional Information from PDB Data
site_idAC1
Number of Residues5
Detailsbinding site for residue EDO A 1101
ChainResidue
AASP787
ATYR813
AASP911
APHE912
A8TN1105

site_idAC2
Number of Residues3
Detailsbinding site for residue EDO A 1102
ChainResidue
ALYS779
AASP911
A8TN1105

site_idAC3
Number of Residues7
Detailsbinding site for residue EDO A 1103
ChainResidue
AGLN170
AASP605
APHE609
AASN640
ALYS642
AHOH1223
APRO168

site_idAC4
Number of Residues7
Detailsbinding site for residue EDO A 1104
ChainResidue
ALEU120
ATRP649
AARG652
AGLY686
AHOH1210
AHOH1251
AHOH1259

site_idAC5
Number of Residues17
Detailsbinding site for residue 8TN A 1105
ChainResidue
APHE751
AMET752
APRO758
ATRP760
AILE777
ATYR813
AILE825
AGLU826
AVAL827
AVAL828
ASER831
AASP832
AMET900
AILE910
AEDO1101
AEDO1102
AHOH1391

Functional Information from PROSITE/UniProt
site_idPS00915
Number of Residues15
DetailsPI3_4_KINASE_1 Phosphatidylinositol 3- and 4-kinases signature 1. FKng.DDLRQDmltlQ
ChainResidueDetails
APHE778-GLN792

site_idPS00916
Number of Residues21
DetailsPI3_4_KINASE_2 Phosphatidylinositol 3- and 4-kinases signature 2. ScAgycVatYVLgIgDRHsdN
ChainResidueDetails
ASER878-ASN898

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsMOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:O00329
ChainResidueDetails
AHIS526

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: Phosphoserine; by autocatalysis => ECO:0000250|UniProtKB:O00329
ChainResidueDetails
AASP1041

223166

PDB entries from 2024-07-31

PDB statisticsPDBj update infoContact PDBjnumon