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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

4JSN

structure of mTORdeltaN-mLST8 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
C0030674molecular_functionprotein-macromolecule adaptor activity
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
C0038203biological_processTORC2 signaling
C0043066biological_processnegative regulation of apoptotic process
C0043491biological_processphosphatidylinositol 3-kinase/protein kinase B signal transduction
C0043539molecular_functionprotein serine/threonine kinase activator activity
C0045821biological_processpositive regulation of glycolytic process
C0046889biological_processpositive regulation of lipid biosynthetic process
C0051897biological_processpositive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction
C0071456biological_processcellular response to hypoxia
C0071470biological_processcellular response to osmotic stress
C1902554cellular_componentserine/threonine protein kinase complex
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
D0030674molecular_functionprotein-macromolecule adaptor activity
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
D0038203biological_processTORC2 signaling
D0043066biological_processnegative regulation of apoptotic process
D0043491biological_processphosphatidylinositol 3-kinase/protein kinase B signal transduction
D0043539molecular_functionprotein serine/threonine kinase activator activity
D0045821biological_processpositive regulation of glycolytic process
D0046889biological_processpositive regulation of lipid biosynthetic process
D0051897biological_processpositive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction
D0071456biological_processcellular response to hypoxia
D0071470biological_processcellular response to osmotic stress
D1902554cellular_componentserine/threonine protein kinase complex
D1905857biological_processpositive regulation of pentose-phosphate shunt
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 Residues66
DetailsRepeat: {"description":"TPR 3"}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues60
DetailsRepeat: {"description":"TPR 4"}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues66
DetailsRepeat: {"description":"TPR 5"}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues66
DetailsRepeat: {"description":"TPR 6"}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues64
DetailsRepeat: {"description":"TPR 7"}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues39
DetailsRepeat: {"description":"TPR 8"}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues68
DetailsRepeat: {"description":"TPR 9"}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues86
DetailsRepeat: {"description":"TPR 10"}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues74
DetailsRepeat: {"description":"TPR 11"}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues108
DetailsRepeat: {"description":"TPR 12"}
ChainResidueDetails
site_idSWS_FT_FI11
Number of Residues64
DetailsRepeat: {"description":"TPR 14"}
ChainResidueDetails
site_idSWS_FT_FI12
Number of Residues78
DetailsRepeat: {"description":"TPR 15"}
ChainResidueDetails
site_idSWS_FT_FI13
Number of Residues68
DetailsRepeat: {"description":"TPR 16"}
ChainResidueDetails
site_idSWS_FT_FI14
Number of Residues64
DetailsDomain: {"description":"FATC","evidences":[{"source":"PROSITE-ProRule","id":"PRU00534","evidenceCode":"ECO:0000255"},{"source":"PROSITE-ProRule","id":"PRU00535","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI15
Number of Residues264
DetailsRegion: {"description":"Sufficient for interaction with the FKBP1A/rapamycin complex","evidences":[{"source":"UniProtKB","id":"Q9JLN9","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI16
Number of Residues12
DetailsRegion: {"description":"G-loop","evidences":[{"source":"PROSITE-ProRule","id":"PRU00269","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI17
Number of Residues76
DetailsRegion: {"description":"Interaction with MLST8"}
ChainResidueDetails
site_idSWS_FT_FI18
Number of Residues16
DetailsRegion: {"description":"Catalytic loop","evidences":[{"source":"PROSITE-ProRule","id":"PRU00269","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI19
Number of Residues50
DetailsRegion: {"description":"Activation loop","evidences":[{"source":"PROSITE-ProRule","id":"PRU00269","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI20
Number of Residues6
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"33158864","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6ZWM","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI21
Number of Residues22
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"29236692","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6BCU","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6BCX","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI22
Number of Residues6
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"29236692","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6BCX","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI23
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine; by TBK1","evidences":[{"source":"PubMed","id":"21576368","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"29150432","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI24
Number of Residues2
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"21576368","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI25
Number of Residues2
DetailsModified residue: {"description":"Phosphothreonine; by PKB/AKT1","evidences":[{"source":"PubMed","id":"24247430","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI26
Number of Residues4
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"source":"PubMed","id":"37979583","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI27
Number of Residues80
DetailsRepeat: {"description":"WD 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00221","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"23636326","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI28
Number of Residues78
DetailsRepeat: {"description":"WD 3","evidences":[{"source":"PROSITE-ProRule","id":"PRU00221","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"23636326","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI29
Number of Residues78
DetailsRepeat: {"description":"WD 4","evidences":[{"source":"PROSITE-ProRule","id":"PRU00221","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"23636326","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI30
Number of Residues78
DetailsRepeat: {"description":"WD 5","evidences":[{"source":"PROSITE-ProRule","id":"PRU00221","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"23636326","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI31
Number of Residues78
DetailsRepeat: {"description":"WD 6","evidences":[{"source":"PROSITE-ProRule","id":"PRU00221","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"23636326","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI32
Number of Residues82
DetailsRepeat: {"description":"WD 7","evidences":[{"source":"PROSITE-ProRule","id":"PRU00221","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"23636326","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI33
Number of Residues2
DetailsModified residue: {"description":"Phosphothreonine; by CDK1","evidences":[{"source":"PubMed","id":"34741373","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI34
Number of Residues8
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO3)","evidences":[{"source":"PubMed","id":"38395307","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI35
Number of Residues6
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate","evidences":[{"source":"PubMed","id":"28489822","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

239149

PDB entries from 2025-07-23

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