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5WBU

Crystal structure of mTOR(deltaN)-mLST8-PRAS40(alpha-helix & beta-strand) complex

Functional Information from GO Data
ChainGOidnamespacecontents
A0004674molecular_functionprotein serine/threonine kinase activity
A0016301molecular_functionkinase activity
A0044877molecular_functionprotein-containing complex binding
B0004674molecular_functionprotein serine/threonine kinase activity
B0016301molecular_functionkinase activity
B0044877molecular_functionprotein-containing complex binding
C0005515molecular_functionprotein binding
C0005654cellular_componentnucleoplasm
C0005737cellular_componentcytoplasm
C0005764cellular_componentlysosome
C0005765cellular_componentlysosomal membrane
C0005829cellular_componentcytosol
C0006974biological_processDNA damage response
C0007010biological_processcytoskeleton organization
C0010507biological_processnegative regulation of autophagy
C0016020cellular_componentmembrane
C0030307biological_processpositive regulation of cell growth
C0030838biological_processpositive regulation of actin filament polymerization
C0031669biological_processcellular response to nutrient levels
C0031929biological_processTOR signaling
C0031931cellular_componentTORC1 complex
C0031932cellular_componentTORC2 complex
C0032008biological_processpositive regulation of TOR signaling
C0032956biological_processregulation of actin cytoskeleton organization
C0038202biological_processTORC1 signaling
C0043066biological_processnegative regulation of apoptotic process
C0043539molecular_functionprotein serine/threonine kinase activator activity
C0045821biological_processpositive regulation of glycolytic process
C0046889biological_processpositive regulation of lipid biosynthetic process
C0050731biological_processpositive regulation of peptidyl-tyrosine phosphorylation
C0071456biological_processcellular response to hypoxia
C0071470biological_processcellular response to osmotic stress
C1905857biological_processpositive regulation of pentose-phosphate shunt
D0005515molecular_functionprotein binding
D0005654cellular_componentnucleoplasm
D0005737cellular_componentcytoplasm
D0005764cellular_componentlysosome
D0005765cellular_componentlysosomal membrane
D0005829cellular_componentcytosol
D0006974biological_processDNA damage response
D0007010biological_processcytoskeleton organization
D0010507biological_processnegative regulation of autophagy
D0016020cellular_componentmembrane
D0030307biological_processpositive regulation of cell growth
D0030838biological_processpositive regulation of actin filament polymerization
D0031669biological_processcellular response to nutrient levels
D0031929biological_processTOR signaling
D0031931cellular_componentTORC1 complex
D0031932cellular_componentTORC2 complex
D0032008biological_processpositive regulation of TOR signaling
D0032956biological_processregulation of actin cytoskeleton organization
D0038202biological_processTORC1 signaling
D0043066biological_processnegative regulation of apoptotic process
D0043539molecular_functionprotein serine/threonine kinase activator activity
D0045821biological_processpositive regulation of glycolytic process
D0046889biological_processpositive regulation of lipid biosynthetic process
D0050731biological_processpositive regulation of peptidyl-tyrosine phosphorylation
D0071456biological_processcellular response to hypoxia
D0071470biological_processcellular response to osmotic stress
D1905857biological_processpositive regulation of pentose-phosphate shunt
O0032007biological_processnegative regulation of TOR signaling
O0048011biological_processneurotrophin TRK receptor signaling pathway
P0032007biological_processnegative regulation of TOR signaling
P0048011biological_processneurotrophin TRK receptor signaling pathway
Q0032007biological_processnegative regulation of TOR signaling
Q0048011biological_processneurotrophin TRK receptor signaling pathway
R0032007biological_processnegative regulation of TOR signaling
R0048011biological_processneurotrophin TRK receptor signaling pathway
Functional Information from PROSITE/UniProt
site_idPS00678
Number of Residues15
DetailsWD_REPEATS_1 Trp-Asp (WD) repeats signature. MYTGgeDcTARIWDL
ChainResidueDetails
DMET100-LEU114

site_idPS00915
Number of Residues15
DetailsPI3_4_KINASE_1 Phosphatidylinositol 3- and 4-kinases signature 1. LKgh.EDLRQDervmQ
ChainResidueDetails
BLEU2186-GLN2200

site_idPS00916
Number of Residues21
DetailsPI3_4_KINASE_2 Phosphatidylinositol 3- and 4-kinases signature 2. SlAvmsMvgYILgLgDRHpsN
ChainResidueDetails
BSER2323-ASN2343

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsMOD_RES: Phosphoserine; by MTOR => ECO:0000269|PubMed:17517883, ECO:0000269|PubMed:18372248, ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163
ChainResidueDetails
PSER183
BMET2345
BILE2356
ASER2165
AGLN2167
ALEU2185
AGLU2190
ATYR2225
AGLY2238
ATRP2239
AVAL2240
RSER183
ATHR2245
AMET2345
AILE2356
OSER183
QSER183
BTYR2225
BGLY2238
BTRP2239
BVAL2240
BTHR2245

site_idSWS_FT_FI2
Number of Residues4
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:24275569
ChainResidueDetails
PSER202
RSER202
OSER202
QSER202
AASN2343
AASP2357

site_idSWS_FT_FI3
Number of Residues4
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569
ChainResidueDetails
PSER203
RSER203
OSER203
QSER203

site_idSWS_FT_FI4
Number of Residues4
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231
ChainResidueDetails
PSER211
RSER211
OSER211
QSER211

site_idSWS_FT_FI5
Number of Residues4
DetailsMOD_RES: Phosphoserine; by MTOR => ECO:0000269|PubMed:18372248, ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163
ChainResidueDetails
PSER212
RSER212
OSER212
QSER212

site_idSWS_FT_FI6
Number of Residues4
DetailsMOD_RES: Phosphoserine; by MTOR => ECO:0000269|PubMed:18372248
ChainResidueDetails
PSER221
RSER221
OSER221
QSER221

site_idSWS_FT_FI7
Number of Residues4
DetailsMOD_RES: Phosphothreonine; by PKB/AKT1 and DYRK3 => ECO:0000269|PubMed:12524439, ECO:0000269|PubMed:23415227, ECO:0000269|PubMed:29634919, ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692
ChainResidueDetails
PTHR246
RTHR246
OTHR246
QTHR246

site_idSWS_FT_FI8
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648
ChainResidueDetails
BSER2478
ASER2478

site_idSWS_FT_FI9
Number of Residues2
DetailsMOD_RES: Phosphoserine; by autocatalysis => ECO:0000269|PubMed:21576368, ECO:0007744|PubMed:18669648
ChainResidueDetails
BSER2481
ASER2481

218853

PDB entries from 2024-04-24

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