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1E8X

STRUCTURAL INSIGHTS INTO PHOSHOINOSITIDE 3-KINASE ENZYMATIC MECHANISM AND SIGNALLING

Replaces:  1QMM
Functional Information from GO Data
ChainGOidnamespacecontents
A0016301molecular_functionkinase activity
A0046854biological_processphosphatidylinositol phosphate biosynthetic process
Functional Information from PDB Data
site_idAC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE LU A3001
ChainResidue
AASN951
AASP964
AATP3000

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE LU A3002
ChainResidue
AHOH2080
AHOH2171
ALU3003
ALU3004

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE LU A3003
ChainResidue
ALU3002
ALU3004
AHOH2011
AHOH2171

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE LU A3004
ChainResidue
AHOH2011
AHOH2081
AHOH2175
ALU3002
ALU3003

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE LU A3005
ChainResidue
AASP836
AASP964
AHOH2193
AATP3000

site_idAC6
Number of Residues2
DetailsBINDING SITE FOR RESIDUE LU A3006
ChainResidue
AASP161
AASP164

site_idAC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE LU A3007
ChainResidue
AASP358
AASP884
ALU3008
ALU3009

site_idAC8
Number of Residues2
DetailsBINDING SITE FOR RESIDUE LU A3008
ChainResidue
AASP358
ALU3007

site_idAC9
Number of Residues2
DetailsBINDING SITE FOR RESIDUE LU A3009
ChainResidue
AHOH2089
ALU3007

site_idBC1
Number of Residues18
DetailsBINDING SITE FOR RESIDUE ATP A3000
ChainResidue
AMET804
ASER806
ALYS807
ALYS808
APRO810
AILE831
ALYS833
AASP836
ATYR867
AGLU880
AVAL882
AASN951
AMET953
AILE963
AASP964
AHOH2253
ALU3001
ALU3005

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:0000269|PubMed:11090628
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:0000250|UniProtKB:P48736
ChainResidueDetails
ASER1101

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PDB entries from 2024-11-06

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