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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

9ED8

Intermediate state of mTOR on membrane

Functional Information from GO Data
ChainGOidnamespacecontents
A0000139cellular_componentGolgi membrane
A0000166molecular_functionnucleotide binding
A0000822molecular_functioninositol hexakisphosphate binding
A0001002molecular_functionRNA polymerase III type 1 promoter sequence-specific DNA binding
A0001003molecular_functionRNA polymerase III type 2 promoter sequence-specific DNA binding
A0001006molecular_functionRNA polymerase III type 3 promoter sequence-specific DNA binding
A0001156molecular_functionTFIIIC-class transcription factor complex binding
A0001558biological_processregulation of cell growth
A0002296biological_processT-helper 1 cell lineage commitment
A0004672molecular_functionprotein kinase activity
A0004674molecular_functionprotein serine/threonine kinase activity
A0004713molecular_functionprotein tyrosine kinase activity
A0004715molecular_functionnon-membrane spanning protein tyrosine kinase activity
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0005634cellular_componentnucleus
A0005635cellular_componentnuclear envelope
A0005654cellular_componentnucleoplasm
A0005737cellular_componentcytoplasm
A0005741cellular_componentmitochondrial outer membrane
A0005764cellular_componentlysosome
A0005765cellular_componentlysosomal membrane
A0005783cellular_componentendoplasmic reticulum
A0005789cellular_componentendoplasmic reticulum membrane
A0005794cellular_componentGolgi apparatus
A0005829cellular_componentcytosol
A0005886cellular_componentplasma membrane
A0006207biological_process'de novo' pyrimidine nucleobase biosynthetic process
A0006468biological_processprotein phosphorylation
A0006954biological_processinflammatory response
A0006974biological_processDNA damage response
A0007010biological_processcytoskeleton organization
A0008361biological_processregulation of cell size
A0009267biological_processcellular response to starvation
A0009408biological_processresponse to heat
A0009891biological_processpositive regulation of biosynthetic process
A0010506biological_processregulation of autophagy
A0010507biological_processnegative regulation of autophagy
A0010718biological_processpositive regulation of epithelial to mesenchymal transition
A0012505cellular_componentendomembrane system
A0016020cellular_componentmembrane
A0016241biological_processregulation of macroautophagy
A0016242biological_processnegative regulation of macroautophagy
A0016301molecular_functionkinase activity
A0016605cellular_componentPML body
A0016740molecular_functiontransferase activity
A0019216biological_processregulation of lipid metabolic process
A0019228biological_processneuronal action potential
A0030307biological_processpositive regulation of cell growth
A0030425cellular_componentdendrite
A0031295biological_processT cell costimulation
A0031410cellular_componentcytoplasmic vesicle
A0031667biological_processresponse to nutrient levels
A0031669biological_processcellular response to nutrient levels
A0031670biological_processcellular response to nutrient
A0031929biological_processTOR signaling
A0031931cellular_componentTORC1 complex
A0031932cellular_componentTORC2 complex
A0032869biological_processcellular response to insulin stimulus
A0032956biological_processregulation of actin cytoskeleton organization
A0034198biological_processcellular response to amino acid starvation
A0038202biological_processTORC1 signaling
A0038203biological_processTORC2 signaling
A0042752biological_processregulation of circadian rhythm
A0042802molecular_functionidentical protein binding
A0043022molecular_functionribosome binding
A0043066biological_processnegative regulation of apoptotic process
A0043200biological_processresponse to amino acid
A0043276biological_processanoikis
A0043491biological_processphosphatidylinositol 3-kinase/protein kinase B signal transduction
A0044325molecular_functiontransmembrane transporter binding
A0045335cellular_componentphagocytic vesicle
A0045597biological_processpositive regulation of cell differentiation
A0045670biological_processregulation of osteoclast differentiation
A0045727biological_processpositive regulation of translation
A0045821biological_processpositive regulation of glycolytic process
A0045860biological_processpositive regulation of protein kinase activity
A0045945biological_processpositive regulation of transcription by RNA polymerase III
A0045948biological_processpositive regulation of translational initiation
A0046627biological_processnegative regulation of insulin receptor signaling pathway
A0046889biological_processpositive regulation of lipid biosynthetic process
A0048266biological_processbehavioral response to pain
A0050821biological_processprotein stabilization
A0051219molecular_functionphosphoprotein binding
A0051240biological_processpositive regulation of multicellular organismal process
A0051549biological_processpositive regulation of keratinocyte migration
A0051896biological_processregulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction
A0051897biological_processpositive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction
A0055006biological_processcardiac cell development
A0061431biological_processcellular response to methionine
A0062027biological_processpositive regulation of SCF-dependent proteasomal ubiquitin-dependent catabolic process
A0071230biological_processcellular response to amino acid stimulus
A0071233biological_processcellular response to L-leucine
A0071456biological_processcellular response to hypoxia
A0071470biological_processcellular response to osmotic stress
A0080135biological_processregulation of cellular response to stress
A0097700biological_processvascular endothelial cell response to laminar fluid shear stress
A0106310molecular_functionprotein serine kinase activity
A1900034biological_processregulation of cellular response to heat
A1900181biological_processnegative regulation of protein localization to nucleus
A1901796biological_processregulation of signal transduction by p53 class mediator
A1901838biological_processpositive regulation of transcription of nucleolar large rRNA by RNA polymerase I
A1903691biological_processpositive regulation of wound healing, spreading of epidermal cells
A1904059biological_processregulation of locomotor rhythm
A1904690biological_processpositive regulation of cytoplasmic translational initiation
A1905671biological_processregulation of lysosome organization
A1905672biological_processnegative regulation of lysosome organization
A1905857biological_processpositive regulation of pentose-phosphate shunt
A1990253biological_processcellular response to leucine starvation
A2000060biological_processpositive regulation of ubiquitin-dependent protein catabolic process
A2000785biological_processregulation of autophagosome assembly
B0004674molecular_functionprotein serine/threonine kinase activity
B0005515molecular_functionprotein binding
B0005654cellular_componentnucleoplasm
B0005737cellular_componentcytoplasm
B0005765cellular_componentlysosomal membrane
B0005829cellular_componentcytosol
B0006974biological_processDNA damage response
B0007010biological_processcytoskeleton organization
B0010507biological_processnegative regulation of autophagy
B0030307biological_processpositive regulation of cell growth
B0030674molecular_functionprotein-macromolecule adaptor activity
B0031669biological_processcellular response to nutrient levels
B0031929biological_processTOR signaling
B0031931cellular_componentTORC1 complex
B0031932cellular_componentTORC2 complex
B0032008biological_processpositive regulation of TOR signaling
B0032956biological_processregulation of actin cytoskeleton organization
B0038202biological_processTORC1 signaling
B0038203biological_processTORC2 signaling
B0043066biological_processnegative regulation of apoptotic process
B0043539molecular_functionprotein serine/threonine kinase activator activity
B0045821biological_processpositive regulation of glycolytic process
B0046889biological_processpositive regulation of lipid biosynthetic process
B0071456biological_processcellular response to hypoxia
B0071470biological_processcellular response to osmotic stress
B1905857biological_processpositive regulation of pentose-phosphate shunt
L0000139cellular_componentGolgi membrane
L0000166molecular_functionnucleotide binding
L0000287molecular_functionmagnesium ion binding
L0003924molecular_functionGTPase activity
L0005515molecular_functionprotein binding
L0005525molecular_functionGTP binding
L0005681cellular_componentspliceosomal complex
L0005765cellular_componentlysosomal membrane
L0005789cellular_componentendoplasmic reticulum membrane
L0005829cellular_componentcytosol
L0005886cellular_componentplasma membrane
L0007165biological_processsignal transduction
L0007264biological_processsmall GTPase-mediated signal transduction
L0012505cellular_componentendomembrane system
L0014069cellular_componentpostsynaptic density
L0016020cellular_componentmembrane
L0016241biological_processregulation of macroautophagy
L0016787molecular_functionhydrolase activity
L0019003molecular_functionGDP binding
L0019901molecular_functionprotein kinase binding
L0030295molecular_functionprotein kinase activator activity
L0031669biological_processcellular response to nutrient levels
L0032006biological_processregulation of TOR signaling
L0032008biological_processpositive regulation of TOR signaling
L0043539molecular_functionprotein serine/threonine kinase activator activity
L0045202cellular_componentsynapse
L0046872molecular_functionmetal ion binding
L0051726biological_processregulation of cell cycle
L0070062cellular_componentextracellular exosome
L0120163biological_processnegative regulation of cold-induced thermogenesis
L1904263biological_processpositive regulation of TORC1 signaling
L2000074biological_processregulation of type B pancreatic cell development
Functional Information from PROSITE/UniProt
site_idPS00678
Number of Residues15
DetailsWD_REPEATS_1 Trp-Asp (WD) repeats signature. MYTGgeDcTARIWDL
ChainResidueDetails
BMET100-LEU114
site_idPS00915
Number of Residues15
DetailsPI3_4_KINASE_1 Phosphatidylinositol 3- and 4-kinases signature 1. LKgh.EDLRQDervmQ
ChainResidueDetails
ALEU2186-GLN2200
site_idPS00916
Number of Residues21
DetailsPI3_4_KINASE_2 Phosphatidylinositol 3- and 4-kinases signature 2. SlAvmsMvgYILgLgDRHpsN
ChainResidueDetails
ASER2323-ASN2343
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues37
DetailsRepeat: {"description":"HEAT 1"}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues44
DetailsRepeat: {"description":"HEAT 2"}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues37
DetailsRepeat: {"description":"HEAT 3"}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues41
DetailsRepeat: {"description":"HEAT 4"}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues40
DetailsRepeat: {"description":"HEAT 5"}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues54
DetailsRepeat: {"description":"HEAT 6"}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues44
DetailsRepeat: {"description":"HEAT 9"}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues35
DetailsRepeat: {"description":"HEAT 10"}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues34
DetailsRepeat: {"description":"HEAT 12"}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues39
DetailsRepeat: {"description":"HEAT 15"}
ChainResidueDetails
site_idSWS_FT_FI11
Number of Residues46
DetailsRepeat: {"description":"HEAT 16"}
ChainResidueDetails
site_idSWS_FT_FI12
Number of Residues38
DetailsRepeat: {"description":"HEAT 17"}
ChainResidueDetails
site_idSWS_FT_FI13
Number of Residues39
DetailsRepeat: {"description":"HEAT 18"}
ChainResidueDetails
site_idSWS_FT_FI14
Number of Residues42
DetailsRepeat: {"description":"HEAT 19"}
ChainResidueDetails
site_idSWS_FT_FI15
Number of Residues39
DetailsRepeat: {"description":"HEAT 20"}
ChainResidueDetails
site_idSWS_FT_FI16
Number of Residues36
DetailsRepeat: {"description":"HEAT 21"}
ChainResidueDetails
site_idSWS_FT_FI17
Number of Residues45
DetailsRepeat: {"description":"HEAT 23"}
ChainResidueDetails
site_idSWS_FT_FI18
Number of Residues38
DetailsRepeat: {"description":"HEAT 24"}
ChainResidueDetails
site_idSWS_FT_FI19
Number of Residues39
DetailsRepeat: {"description":"HEAT 25"}
ChainResidueDetails
site_idSWS_FT_FI20
Number of Residues36
DetailsRepeat: {"description":"HEAT 26"}
ChainResidueDetails
site_idSWS_FT_FI21
Number of Residues38
DetailsRepeat: {"description":"HEAT 27"}
ChainResidueDetails
site_idSWS_FT_FI22
Number of Residues43
DetailsRepeat: {"description":"HEAT 28"}
ChainResidueDetails
site_idSWS_FT_FI23
Number of Residues37
DetailsRepeat: {"description":"HEAT 31"}
ChainResidueDetails
site_idSWS_FT_FI24
Number of Residues33
DetailsRepeat: {"description":"HEAT 32"}
ChainResidueDetails
site_idSWS_FT_FI25
Number of Residues36
DetailsRepeat: {"description":"TPR 1"}
ChainResidueDetails
site_idSWS_FT_FI26
Number of Residues25
DetailsRepeat: {"description":"TPR 2"}
ChainResidueDetails
site_idSWS_FT_FI27
Number of Residues33
DetailsRepeat: {"description":"TPR 3"}
ChainResidueDetails
site_idSWS_FT_FI28
Number of Residues30
DetailsRepeat: {"description":"TPR 4"}
ChainResidueDetails
site_idSWS_FT_FI29
Number of Residues33
DetailsRepeat: {"description":"TPR 5"}
ChainResidueDetails
site_idSWS_FT_FI30
Number of Residues33
DetailsRepeat: {"description":"TPR 6"}
ChainResidueDetails
site_idSWS_FT_FI31
Number of Residues32
DetailsRepeat: {"description":"TPR 7"}
ChainResidueDetails
site_idSWS_FT_FI32
Number of Residues39
DetailsRepeat: {"description":"TPR 8"}
ChainResidueDetails
site_idSWS_FT_FI33
Number of Residues34
DetailsRepeat: {"description":"TPR 9"}
ChainResidueDetails
site_idSWS_FT_FI34
Number of Residues43
DetailsRepeat: {"description":"TPR 10"}
ChainResidueDetails
site_idSWS_FT_FI35
Number of Residues37
DetailsRepeat: {"description":"TPR 11"}
ChainResidueDetails
site_idSWS_FT_FI36
Number of Residues54
DetailsRepeat: {"description":"TPR 12"}
ChainResidueDetails
site_idSWS_FT_FI37
Number of Residues32
DetailsRepeat: {"description":"TPR 14"}
ChainResidueDetails
site_idSWS_FT_FI38
Number of Residues39
DetailsRepeat: {"description":"TPR 15"}
ChainResidueDetails
site_idSWS_FT_FI39
Number of Residues34
DetailsRepeat: {"description":"TPR 16"}
ChainResidueDetails
site_idSWS_FT_FI40
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_FI41
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_FI42
Number of Residues6
DetailsRegion: {"description":"G-loop","evidences":[{"source":"PROSITE-ProRule","id":"PRU00269","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI43
Number of Residues38
DetailsRegion: {"description":"Interaction with MLST8"}
ChainResidueDetails
site_idSWS_FT_FI44
Number of Residues8
DetailsRegion: {"description":"Catalytic loop","evidences":[{"source":"PROSITE-ProRule","id":"PRU00269","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI45
Number of Residues25
DetailsRegion: {"description":"Activation loop","evidences":[{"source":"PROSITE-ProRule","id":"PRU00269","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI46
Number of Residues3
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"33158864","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6ZWM","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI47
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_FI48
Number of Residues3
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"29236692","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6BCX","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI49
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"20068231","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI50
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"19487463","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI51
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_FI52
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"21576368","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI53
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine; by PKB/AKT1","evidences":[{"source":"PubMed","id":"24247430","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":"37979583","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI55
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_FI56
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_FI57
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_FI58
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_FI59
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_FI60
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_FI61
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine; by CDK1","evidences":[{"source":"PubMed","id":"34741373","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI62
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_FI63
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_FI64
Number of Residues8
DetailsMotif: {"description":"Effector region","evidences":[{"evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI65
Number of Residues6
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"15728574","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"29236692","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1XTS","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6BCU","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI66
Number of Residues1
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"15728574","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22002721","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22819219","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"32470140","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1XTQ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3SEA","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3T5G","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7BTA","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7BTC","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI67
Number of Residues1
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"15728574","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22002721","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"29236692","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1XTS","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6BCU","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI68
Number of Residues1
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"15728574","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"29236692","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"29416044","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5YXH","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6BCU","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6BSX","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6BT0","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI69
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"15728574","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1XTS","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI70
Number of Residues1
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"15728574","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22002721","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22819219","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"29416044","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"32470140","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3SEA","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6BT0","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7BTA","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7BTC","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI71
Number of Residues1
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"15728574","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"29236692","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6BCU","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI72
Number of Residues1
DetailsSite: {"description":"Important for autoinhibition of GTPase activity","evidences":[{"source":"PubMed","id":"22819219","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI73
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine; by MAPKAPK5","evidences":[{"source":"UniProtKB","id":"Q921J2","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI74
Number of Residues2
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"source":"PubMed","id":"30514904","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

247536

PDB entries from 2026-01-14

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