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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

6BSX

CRYSTAL STRUCTURE OF RHEB IN COMPLEX WITH COMPOUND 1 AT 1.65A RESOLUTION

Functional Information from GO Data
ChainGOidnamespacecontents
A0000139cellular_componentGolgi membrane
A0000166molecular_functionnucleotide binding
A0000287molecular_functionmagnesium ion binding
A0003924molecular_functionGTPase activity
A0005515molecular_functionprotein binding
A0005525molecular_functionGTP binding
A0005681cellular_componentspliceosomal complex
A0005765cellular_componentlysosomal membrane
A0005789cellular_componentendoplasmic reticulum membrane
A0005829cellular_componentcytosol
A0005886cellular_componentplasma membrane
A0007165biological_processsignal transduction
A0007264biological_processsmall GTPase-mediated signal transduction
A0012505cellular_componentendomembrane system
A0014069cellular_componentpostsynaptic density
A0016020cellular_componentmembrane
A0016241biological_processregulation of macroautophagy
A0016787molecular_functionhydrolase activity
A0019003molecular_functionGDP binding
A0019901molecular_functionprotein kinase binding
A0030295molecular_functionprotein kinase activator activity
A0031669biological_processcellular response to nutrient levels
A0032006biological_processregulation of TOR signaling
A0032008biological_processpositive regulation of TOR signaling
A0043539molecular_functionprotein serine/threonine kinase activator activity
A0045202cellular_componentsynapse
A0046872molecular_functionmetal ion binding
A0051726biological_processregulation of cell cycle
A0070062cellular_componentextracellular exosome
A0120163biological_processnegative regulation of cold-induced thermogenesis
A1904263biological_processpositive regulation of TORC1 signaling
A2000074biological_processregulation of type B pancreatic cell development
B0000139cellular_componentGolgi membrane
B0000166molecular_functionnucleotide binding
B0000287molecular_functionmagnesium ion binding
B0003924molecular_functionGTPase activity
B0005515molecular_functionprotein binding
B0005525molecular_functionGTP binding
B0005681cellular_componentspliceosomal complex
B0005765cellular_componentlysosomal membrane
B0005789cellular_componentendoplasmic reticulum membrane
B0005829cellular_componentcytosol
B0005886cellular_componentplasma membrane
B0007165biological_processsignal transduction
B0007264biological_processsmall GTPase-mediated signal transduction
B0012505cellular_componentendomembrane system
B0014069cellular_componentpostsynaptic density
B0016020cellular_componentmembrane
B0016241biological_processregulation of macroautophagy
B0016787molecular_functionhydrolase activity
B0019003molecular_functionGDP binding
B0019901molecular_functionprotein kinase binding
B0030295molecular_functionprotein kinase activator activity
B0031669biological_processcellular response to nutrient levels
B0032006biological_processregulation of TOR signaling
B0032008biological_processpositive regulation of TOR signaling
B0043539molecular_functionprotein serine/threonine kinase activator activity
B0045202cellular_componentsynapse
B0046872molecular_functionmetal ion binding
B0051726biological_processregulation of cell cycle
B0070062cellular_componentextracellular exosome
B0120163biological_processnegative regulation of cold-induced thermogenesis
B1904263biological_processpositive regulation of TORC1 signaling
B2000074biological_processregulation of type B pancreatic cell development
C0000139cellular_componentGolgi membrane
C0000166molecular_functionnucleotide binding
C0000287molecular_functionmagnesium ion binding
C0003924molecular_functionGTPase activity
C0005515molecular_functionprotein binding
C0005525molecular_functionGTP binding
C0005681cellular_componentspliceosomal complex
C0005765cellular_componentlysosomal membrane
C0005789cellular_componentendoplasmic reticulum membrane
C0005829cellular_componentcytosol
C0005886cellular_componentplasma membrane
C0007165biological_processsignal transduction
C0007264biological_processsmall GTPase-mediated signal transduction
C0012505cellular_componentendomembrane system
C0014069cellular_componentpostsynaptic density
C0016020cellular_componentmembrane
C0016241biological_processregulation of macroautophagy
C0016787molecular_functionhydrolase activity
C0019003molecular_functionGDP binding
C0019901molecular_functionprotein kinase binding
C0030295molecular_functionprotein kinase activator activity
C0031669biological_processcellular response to nutrient levels
C0032006biological_processregulation of TOR signaling
C0032008biological_processpositive regulation of TOR signaling
C0043539molecular_functionprotein serine/threonine kinase activator activity
C0045202cellular_componentsynapse
C0046872molecular_functionmetal ion binding
C0051726biological_processregulation of cell cycle
C0070062cellular_componentextracellular exosome
C0120163biological_processnegative regulation of cold-induced thermogenesis
C1904263biological_processpositive regulation of TORC1 signaling
C2000074biological_processregulation of type B pancreatic cell development
D0000139cellular_componentGolgi membrane
D0000166molecular_functionnucleotide binding
D0000287molecular_functionmagnesium ion binding
D0003924molecular_functionGTPase activity
D0005515molecular_functionprotein binding
D0005525molecular_functionGTP binding
D0005681cellular_componentspliceosomal complex
D0005765cellular_componentlysosomal membrane
D0005789cellular_componentendoplasmic reticulum membrane
D0005829cellular_componentcytosol
D0005886cellular_componentplasma membrane
D0007165biological_processsignal transduction
D0007264biological_processsmall GTPase-mediated signal transduction
D0012505cellular_componentendomembrane system
D0014069cellular_componentpostsynaptic density
D0016020cellular_componentmembrane
D0016241biological_processregulation of macroautophagy
D0016787molecular_functionhydrolase activity
D0019003molecular_functionGDP binding
D0019901molecular_functionprotein kinase binding
D0030295molecular_functionprotein kinase activator activity
D0031669biological_processcellular response to nutrient levels
D0032006biological_processregulation of TOR signaling
D0032008biological_processpositive regulation of TOR signaling
D0043539molecular_functionprotein serine/threonine kinase activator activity
D0045202cellular_componentsynapse
D0046872molecular_functionmetal ion binding
D0051726biological_processregulation of cell cycle
D0070062cellular_componentextracellular exosome
D0120163biological_processnegative regulation of cold-induced thermogenesis
D1904263biological_processpositive regulation of TORC1 signaling
D2000074biological_processregulation of type B pancreatic cell development
Functional Information from PDB Data
site_idAC1
Number of Residues6
Detailsbinding site for residue MG A 201
ChainResidue
ASER20
AGDP203
AHOH323
AHOH337
AHOH367
AHOH371
site_idAC2
Number of Residues1
Detailsbinding site for residue ACT A 202
ChainResidue
AGLU28
site_idAC3
Number of Residues24
Detailsbinding site for residue GDP A 203
ChainResidue
AGLY18
ALYS19
ASER20
ASER21
APHE31
AASN119
ALYS120
AASP122
ALEU123
ASER149
AALA150
ALYS151
AMG201
AHOH306
AHOH311
AHOH312
AHOH323
AHOH329
AHOH337
AHOH371
AHOH391
AHOH402
ASER16
AVAL17
site_idAC4
Number of Residues11
Detailsbinding site for residue E7S A 204
ChainResidue
AALA10
AGLU40
ATHR61
AALA62
AGLY63
AGLN64
ATYR74
AHOH303
AHOH324
BHIS55
BHOH364
site_idAC5
Number of Residues4
Detailsbinding site for residue EDO A 205
ChainResidue
AILE129
AGLU133
AHOH347
BASP158
site_idAC6
Number of Residues6
Detailsbinding site for residue MG B 201
ChainResidue
BSER20
BGDP203
BHOH316
BHOH320
BHOH365
BHOH368
site_idAC7
Number of Residues2
Detailsbinding site for residue ACT B 202
ChainResidue
BGLU28
BTYR35
site_idAC8
Number of Residues25
Detailsbinding site for residue GDP B 203
ChainResidue
BARG15
BSER16
BVAL17
BGLY18
BLYS19
BSER20
BSER21
BPHE31
BASP33
BASN119
BLYS120
BASP122
BLEU123
BSER149
BALA150
BMG201
BHOH302
BHOH305
BHOH316
BHOH320
BHOH352
BHOH356
BHOH368
BHOH386
BHOH412
site_idAC9
Number of Residues11
Detailsbinding site for residue E7S B 204
ChainResidue
AHIS55
BALA10
BGLU40
BTHR61
BALA62
BGLY63
BGLN64
BTYR74
BHOH304
BHOH323
BHOH362
site_idAD1
Number of Residues3
Detailsbinding site for residue EDO B 205
ChainResidue
AASP158
AHOH317
BGLU133
site_idAD2
Number of Residues6
Detailsbinding site for residue MG C 201
ChainResidue
CSER20
CGDP203
CHOH319
CHOH340
CHOH349
CHOH376
site_idAD3
Number of Residues2
Detailsbinding site for residue ACT C 202
ChainResidue
CGLU28
CTYR35
site_idAD4
Number of Residues25
Detailsbinding site for residue GDP C 203
ChainResidue
CSER16
CVAL17
CGLY18
CLYS19
CSER20
CSER21
CPHE31
CVAL32
CASP33
CASN119
CLYS120
CASP122
CLEU123
CSER149
CALA150
CLYS151
CMG201
CHOH314
CHOH319
CHOH322
CHOH340
CHOH362
CHOH365
CHOH373
CHOH376
site_idAD5
Number of Residues11
Detailsbinding site for residue E7S C 204
ChainResidue
CALA10
CGLU40
CTHR61
CALA62
CGLY63
CGLN64
CTYR74
CHOH307
CHOH335
CHOH358
DHIS55
site_idAD6
Number of Residues3
Detailsbinding site for residue EDO C 205
ChainResidue
CGLU133
CHOH391
DASP158
site_idAD7
Number of Residues6
Detailsbinding site for residue MG D 201
ChainResidue
DSER20
DGDP203
DHOH328
DHOH332
DHOH351
DHOH366
site_idAD8
Number of Residues2
Detailsbinding site for residue ACT D 202
ChainResidue
DGLU28
DTYR35
site_idAD9
Number of Residues24
Detailsbinding site for residue GDP D 203
ChainResidue
DSER16
DVAL17
DGLY18
DLYS19
DSER20
DSER21
DPHE31
DVAL32
DASP33
DASN119
DLYS120
DASP122
DLEU123
DSER149
DALA150
DLYS151
DMG201
DHOH324
DHOH328
DHOH330
DHOH332
DHOH346
DHOH366
DHOH376
site_idAE1
Number of Residues11
Detailsbinding site for residue E7S D 204
ChainResidue
CHIS55
DALA10
DGLU40
DTHR61
DALA62
DGLY63
DGLN64
DPHE70
DTYR74
DHOH301
DHOH306
site_idAE2
Number of Residues4
Detailsbinding site for residue EDO D 205
ChainResidue
CASP158
CHOH347
DGLU133
DHOH388
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues32
DetailsMotif: {"description":"Effector region","evidences":[{"evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues24
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_FI3
Number of Residues4
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_FI4
Number of Residues4
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_FI5
Number of Residues4
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_FI6
Number of Residues8
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"15728574","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1XTS","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues4
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_FI8
Number of Residues4
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_FI9
Number of Residues4
DetailsSite: {"description":"Important for autoinhibition of GTPase activity","evidences":[{"source":"PubMed","id":"22819219","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues4
DetailsModified residue: {"description":"Phosphoserine; by MAPKAPK5","evidences":[{"source":"UniProtKB","id":"Q921J2","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI11
Number of Residues8
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"source":"PubMed","id":"30514904","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

245663

PDB entries from 2025-12-03

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