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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

6ZWO

cryo-EM structure of human mTOR complex 2, focused on one half

Functional Information from GO Data
ChainGOidnamespacecontents
B0000139cellular_componentGolgi membrane
B0000166molecular_functionnucleotide binding
B0000822molecular_functioninositol hexakisphosphate binding
B0001002molecular_functionRNA polymerase III type 1 promoter sequence-specific DNA binding
B0001003molecular_functionRNA polymerase III type 2 promoter sequence-specific DNA binding
B0001006molecular_functionRNA polymerase III type 3 promoter sequence-specific DNA binding
B0001156molecular_functionTFIIIC-class transcription factor complex binding
B0001558biological_processregulation of cell growth
B0002296biological_processT-helper 1 cell lineage commitment
B0004672molecular_functionprotein kinase activity
B0004674molecular_functionprotein serine/threonine kinase activity
B0004713molecular_functionprotein tyrosine kinase activity
B0004715molecular_functionnon-membrane spanning protein tyrosine kinase activity
B0005515molecular_functionprotein binding
B0005524molecular_functionATP binding
B0005634cellular_componentnucleus
B0005635cellular_componentnuclear envelope
B0005654cellular_componentnucleoplasm
B0005737cellular_componentcytoplasm
B0005741cellular_componentmitochondrial outer membrane
B0005764cellular_componentlysosome
B0005765cellular_componentlysosomal membrane
B0005783cellular_componentendoplasmic reticulum
B0005789cellular_componentendoplasmic reticulum membrane
B0005794cellular_componentGolgi apparatus
B0005829cellular_componentcytosol
B0005886cellular_componentplasma membrane
B0006207biological_process'de novo' pyrimidine nucleobase biosynthetic process
B0006468biological_processprotein phosphorylation
B0006954biological_processinflammatory response
B0006974biological_processDNA damage response
B0007010biological_processcytoskeleton organization
B0008361biological_processregulation of cell size
B0009267biological_processcellular response to starvation
B0009408biological_processresponse to heat
B0009891biological_processpositive regulation of biosynthetic process
B0010506biological_processregulation of autophagy
B0010507biological_processnegative regulation of autophagy
B0010718biological_processpositive regulation of epithelial to mesenchymal transition
B0012505cellular_componentendomembrane system
B0016020cellular_componentmembrane
B0016241biological_processregulation of macroautophagy
B0016242biological_processnegative regulation of macroautophagy
B0016301molecular_functionkinase activity
B0016605cellular_componentPML body
B0016740molecular_functiontransferase activity
B0019216biological_processregulation of lipid metabolic process
B0019228biological_processneuronal action potential
B0030307biological_processpositive regulation of cell growth
B0030425cellular_componentdendrite
B0031295biological_processT cell costimulation
B0031410cellular_componentcytoplasmic vesicle
B0031667biological_processresponse to nutrient levels
B0031669biological_processcellular response to nutrient levels
B0031670biological_processcellular response to nutrient
B0031929biological_processTOR signaling
B0031931cellular_componentTORC1 complex
B0031932cellular_componentTORC2 complex
B0032869biological_processcellular response to insulin stimulus
B0032956biological_processregulation of actin cytoskeleton organization
B0034198biological_processcellular response to amino acid starvation
B0038202biological_processTORC1 signaling
B0038203biological_processTORC2 signaling
B0042752biological_processregulation of circadian rhythm
B0042802molecular_functionidentical protein binding
B0043022molecular_functionribosome binding
B0043066biological_processnegative regulation of apoptotic process
B0043200biological_processresponse to amino acid
B0043276biological_processanoikis
B0043491biological_processphosphatidylinositol 3-kinase/protein kinase B signal transduction
B0044325molecular_functiontransmembrane transporter binding
B0044877molecular_functionprotein-containing complex binding
B0045335cellular_componentphagocytic vesicle
B0045597biological_processpositive regulation of cell differentiation
B0045670biological_processregulation of osteoclast differentiation
B0045727biological_processpositive regulation of translation
B0045821biological_processpositive regulation of glycolytic process
B0045860biological_processpositive regulation of protein kinase activity
B0045945biological_processpositive regulation of transcription by RNA polymerase III
B0045948biological_processpositive regulation of translational initiation
B0046627biological_processnegative regulation of insulin receptor signaling pathway
B0046889biological_processpositive regulation of lipid biosynthetic process
B0048266biological_processbehavioral response to pain
B0050821biological_processprotein stabilization
B0051219molecular_functionphosphoprotein binding
B0051240biological_processpositive regulation of multicellular organismal process
B0051549biological_processpositive regulation of keratinocyte migration
B0051896biological_processregulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction
B0051897biological_processpositive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction
B0055006biological_processcardiac cell development
B0061431biological_processcellular response to methionine
B0062027biological_processpositive regulation of SCF-dependent proteasomal ubiquitin-dependent catabolic process
B0071230biological_processcellular response to amino acid stimulus
B0071233biological_processcellular response to L-leucine
B0071456biological_processcellular response to hypoxia
B0071470biological_processcellular response to osmotic stress
B0080135biological_processregulation of cellular response to stress
B0097700biological_processvascular endothelial cell response to laminar fluid shear stress
B0106310molecular_functionprotein serine kinase activity
B1900034biological_processregulation of cellular response to heat
B1900181biological_processnegative regulation of protein localization to nucleus
B1901796biological_processregulation of signal transduction by p53 class mediator
B1901838biological_processpositive regulation of transcription of nucleolar large rRNA by RNA polymerase I
B1903691biological_processpositive regulation of wound healing, spreading of epidermal cells
B1904059biological_processregulation of locomotor rhythm
B1904690biological_processpositive regulation of cytoplasmic translational initiation
B1905671biological_processregulation of lysosome organization
B1905672biological_processnegative regulation of lysosome organization
B1905857biological_processpositive regulation of pentose-phosphate shunt
B1990253biological_processcellular response to leucine starvation
B2000060biological_processpositive regulation of ubiquitin-dependent protein catabolic process
B2000785biological_processregulation of autophagosome assembly
D0004674molecular_functionprotein serine/threonine kinase activity
D0005515molecular_functionprotein binding
D0005654cellular_componentnucleoplasm
D0005737cellular_componentcytoplasm
D0005765cellular_componentlysosomal membrane
D0005829cellular_componentcytosol
D0006974biological_processDNA damage response
D0007010biological_processcytoskeleton organization
D0010507biological_processnegative regulation of autophagy
D0030307biological_processpositive regulation of cell growth
D0030674molecular_functionprotein-macromolecule adaptor activity
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
D0043539molecular_functionprotein serine/threonine kinase activator activity
D0045821biological_processpositive regulation of glycolytic process
D0046889biological_processpositive regulation of lipid biosynthetic process
D0071456biological_processcellular response to hypoxia
D0071470biological_processcellular response to osmotic stress
D1905857biological_processpositive regulation of pentose-phosphate shunt
F0000166molecular_functionnucleotide binding
F0001938biological_processpositive regulation of endothelial cell proliferation
F0004674molecular_functionprotein serine/threonine kinase activity
F0005515molecular_functionprotein binding
F0005524molecular_functionATP binding
F0005764cellular_componentlysosome
F0005765cellular_componentlysosomal membrane
F0005783cellular_componentendoplasmic reticulum
F0005789cellular_componentendoplasmic reticulum membrane
F0005794cellular_componentGolgi apparatus
F0005829cellular_componentcytosol
F0005886cellular_componentplasma membrane
F0007010biological_processcytoskeleton organization
F0008270molecular_functionzinc ion binding
F0008610biological_processlipid biosynthetic process
F0009792biological_processembryo development ending in birth or egg hatching
F0019901molecular_functionprotein kinase binding
F0030036biological_processactin cytoskeleton organization
F0030307biological_processpositive regulation of cell growth
F0030335biological_processpositive regulation of cell migration
F0031669biological_processcellular response to nutrient levels
F0031929biological_processTOR signaling
F0031932cellular_componentTORC2 complex
F0032008biological_processpositive regulation of TOR signaling
F0032956biological_processregulation of actin cytoskeleton organization
F0038203biological_processTORC2 signaling
F0043022molecular_functionribosome binding
F0043066biological_processnegative regulation of apoptotic process
F0043539molecular_functionprotein serine/threonine kinase activator activity
F0051896biological_processregulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction
F0051897biological_processpositive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction
F0060090molecular_functionmolecular adaptor activity
F0140767molecular_functionenzyme-substrate adaptor activity
H0000139cellular_componentGolgi membrane
H0004674molecular_functionprotein serine/threonine kinase activity
H0005515molecular_functionprotein binding
H0005546molecular_functionphosphatidylinositol-4,5-bisphosphate binding
H0005547molecular_functionphosphatidylinositol-3,4,5-trisphosphate binding
H0005634cellular_componentnucleus
H0005654cellular_componentnucleoplasm
H0005737cellular_componentcytoplasm
H0005741cellular_componentmitochondrial outer membrane
H0005764cellular_componentlysosome
H0005765cellular_componentlysosomal membrane
H0005769cellular_componentearly endosome
H0005770cellular_componentlate endosome
H0005783cellular_componentendoplasmic reticulum
H0005789cellular_componentendoplasmic reticulum membrane
H0005794cellular_componentGolgi apparatus
H0005829cellular_componentcytosol
H0005886cellular_componentplasma membrane
H0007010biological_processcytoskeleton organization
H0019901molecular_functionprotein kinase binding
H0021762biological_processsubstantia nigra development
H0030307biological_processpositive regulation of cell growth
H0031267molecular_functionsmall GTPase binding
H0031669biological_processcellular response to nutrient levels
H0031901cellular_componentearly endosome membrane
H0031902cellular_componentlate endosome membrane
H0031932cellular_componentTORC2 complex
H0032869biological_processcellular response to insulin stimulus
H0038203biological_processTORC2 signaling
H0043066biological_processnegative regulation of apoptotic process
H0043325molecular_functionphosphatidylinositol-3,4-bisphosphate binding
H0046580biological_processnegative regulation of Ras protein signal transduction
H0046627biological_processnegative regulation of insulin receptor signaling pathway
H0048471cellular_componentperinuclear region of cytoplasm
H0060090molecular_functionmolecular adaptor activity
H0070300molecular_functionphosphatidic acid binding
H0080025molecular_functionphosphatidylinositol-3,5-bisphosphate binding
H0140767molecular_functionenzyme-substrate adaptor activity
H1900407biological_processregulation of cellular response to oxidative stress
Functional Information from PROSITE/UniProt
site_idPS00307
Number of Residues7
DetailsLECTIN_LEGUME_BETA Legume lectins beta-chain signature. VAVDLDS
ChainResidueDetails
HVAL333-SER339
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 Residues39
DetailsRepeat: {"description":"HEAT 20"}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues36
DetailsRepeat: {"description":"HEAT 21"}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues45
DetailsRepeat: {"description":"HEAT 23"}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues38
DetailsRepeat: {"description":"HEAT 24"}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues39
DetailsRepeat: {"description":"HEAT 25"}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues36
DetailsRepeat: {"description":"HEAT 26"}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues38
DetailsRepeat: {"description":"HEAT 27"}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues43
DetailsRepeat: {"description":"HEAT 28"}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues36
DetailsRepeat: {"description":"HEAT 29"}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues37
DetailsRepeat: {"description":"HEAT 31"}
ChainResidueDetails
site_idSWS_FT_FI11
Number of Residues33
DetailsRepeat: {"description":"HEAT 32"}
ChainResidueDetails
site_idSWS_FT_FI12
Number of Residues36
DetailsRepeat: {"description":"TPR 1"}
ChainResidueDetails
site_idSWS_FT_FI13
Number of Residues25
DetailsRepeat: {"description":"TPR 2"}
ChainResidueDetails
site_idSWS_FT_FI14
Number of Residues33
DetailsRepeat: {"description":"TPR 3"}
ChainResidueDetails
site_idSWS_FT_FI15
Number of Residues30
DetailsRepeat: {"description":"TPR 4"}
ChainResidueDetails
site_idSWS_FT_FI16
Number of Residues33
DetailsRepeat: {"description":"TPR 5"}
ChainResidueDetails
site_idSWS_FT_FI17
Number of Residues33
DetailsRepeat: {"description":"TPR 6"}
ChainResidueDetails
site_idSWS_FT_FI18
Number of Residues32
DetailsRepeat: {"description":"TPR 7"}
ChainResidueDetails
site_idSWS_FT_FI19
Number of Residues39
DetailsRepeat: {"description":"TPR 8"}
ChainResidueDetails
site_idSWS_FT_FI20
Number of Residues34
DetailsRepeat: {"description":"TPR 9"}
ChainResidueDetails
site_idSWS_FT_FI21
Number of Residues43
DetailsRepeat: {"description":"TPR 10"}
ChainResidueDetails
site_idSWS_FT_FI22
Number of Residues37
DetailsRepeat: {"description":"TPR 11"}
ChainResidueDetails
site_idSWS_FT_FI23
Number of Residues54
DetailsRepeat: {"description":"TPR 12"}
ChainResidueDetails
site_idSWS_FT_FI24
Number of Residues32
DetailsRepeat: {"description":"TPR 14"}
ChainResidueDetails
site_idSWS_FT_FI25
Number of Residues39
DetailsRepeat: {"description":"TPR 15"}
ChainResidueDetails
site_idSWS_FT_FI26
Number of Residues34
DetailsRepeat: {"description":"TPR 16"}
ChainResidueDetails
site_idSWS_FT_FI27
Number of Residues32
DetailsDomain: {"description":"FATC","evidences":[{"source":"PROSITE-ProRule","id":"PRU00534","evidenceCode":"ECO:0000255"},{"source":"PROSITE-ProRule","id":"PRU00535","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI28
Number of Residues132
DetailsRegion: {"description":"Sufficient for interaction with the FKBP1A/rapamycin complex","evidences":[{"source":"UniProtKB","id":"Q9JLN9","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI29
Number of Residues6
DetailsRegion: {"description":"G-loop","evidences":[{"source":"PROSITE-ProRule","id":"PRU00269","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI30
Number of Residues38
DetailsRegion: {"description":"Interaction with MLST8"}
ChainResidueDetails
site_idSWS_FT_FI31
Number of Residues8
DetailsRegion: {"description":"Catalytic loop","evidences":[{"source":"PROSITE-ProRule","id":"PRU00269","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI32
Number of Residues25
DetailsRegion: {"description":"Activation loop","evidences":[{"source":"PROSITE-ProRule","id":"PRU00269","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI33
Number of Residues7
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"33158864","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6ZWM","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI34
Number of Residues11
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_FI35
Number of Residues3
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"29236692","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6BCX","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI36
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"20068231","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI37
Number of Residues1
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI38
Number of Residues1
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_FI39
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"21576368","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI40
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine; by PKB/AKT1","evidences":[{"source":"PubMed","id":"24247430","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI41
Number of Residues2
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_FI42
Number of Residues40
DetailsRepeat: {"description":"WD 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00221","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"23636326","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI43
Number of Residues39
DetailsRepeat: {"description":"WD 3","evidences":[{"source":"PROSITE-ProRule","id":"PRU00221","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"23636326","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI44
Number of Residues39
DetailsRepeat: {"description":"WD 4","evidences":[{"source":"PROSITE-ProRule","id":"PRU00221","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"23636326","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI45
Number of Residues39
DetailsRepeat: {"description":"WD 5","evidences":[{"source":"PROSITE-ProRule","id":"PRU00221","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"23636326","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI46
Number of Residues39
DetailsRepeat: {"description":"WD 6","evidences":[{"source":"PROSITE-ProRule","id":"PRU00221","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"23636326","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI47
Number of Residues41
DetailsRepeat: {"description":"WD 7","evidences":[{"source":"PROSITE-ProRule","id":"PRU00221","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"23636326","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI48
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine; by CDK1","evidences":[{"source":"PubMed","id":"34741373","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI49
Number of Residues4
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_FI50
Number of Residues3
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate","evidences":[{"source":"PubMed","id":"28489822","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI51
Number of Residues49
DetailsRegion: {"description":"Ribosome-binding domain","evidences":[{"source":"PubMed","id":"26176550","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI52
Number of Residues3
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"33158864","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"6ZWM","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI53
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"19720745","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI54
Number of Residues2
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"source":"PubMed","id":"33378666","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI55
Number of Residues1
DetailsModified residue: {"description":"N-acetylalanine","evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"MAR-2009","submissionDatabase":"UniProtKB","authors":["Bienvenut W.V.","Waridel P.","Quadroni M."]}}]}
ChainResidueDetails
site_idSWS_FT_FI56
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"Q8BKH7","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI57
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"Q8BKH7","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

247536

PDB entries from 2026-01-14

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