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3SEA

Structure of Rheb-Y35A mutant in GDP- and GMPPNP-bound forms

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
A0005737cellular_componentcytoplasm
A0005764cellular_componentlysosome
A0005765cellular_componentlysosomal membrane
A0005783cellular_componentendoplasmic reticulum
A0005789cellular_componentendoplasmic reticulum membrane
A0005794cellular_componentGolgi apparatus
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
A0048709biological_processoligodendrocyte differentiation
A0048714biological_processpositive regulation of oligodendrocyte differentiation
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
B0005737cellular_componentcytoplasm
B0005764cellular_componentlysosome
B0005765cellular_componentlysosomal membrane
B0005783cellular_componentendoplasmic reticulum
B0005789cellular_componentendoplasmic reticulum membrane
B0005794cellular_componentGolgi apparatus
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
B0048709biological_processoligodendrocyte differentiation
B0048714biological_processpositive regulation of oligodendrocyte differentiation
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
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG A 202
ChainResidue
ASER20
AHOH170
AHOH172
AHOH176
AHOH197
AGDP201

site_idAC2
Number of Residues23
DetailsBINDING SITE FOR RESIDUE GDP A 201
ChainResidue
ALYS19
ASER20
ASER21
APHE31
AVAL32
AASP33
AASN119
ALYS120
AASP122
ALEU123
ASER149
AALA150
AHOH172
AHOH189
AHOH197
AMG202
AHOH235
AHOH269
AHOH273
AHOH290
ASER16
AVAL17
AGLY18

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG B 178
ChainResidue
BSER20
BTHR38
BHOH174
BGNP179
BHOH262

site_idAC4
Number of Residues25
DetailsBINDING SITE FOR RESIDUE GNP B 179
ChainResidue
BARG15
BSER16
BVAL17
BGLY18
BLYS19
BSER20
BSER21
BPHE31
BVAL32
BASP33
BALA35
BPRO37
BTHR38
BGLY63
BASN119
BLYS120
BASP122
BLEU123
BSER149
BALA150
BHOH174
BMG178
BHOH215
BHOH262
BHOH289

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ACT B 1
ChainResidue
BALA35
BASP36
BTHR38
BASN41
BHOH267

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues12
DetailsBINDING: BINDING => ECO:0000269|PubMed:15728574, ECO:0000269|PubMed:29236692, ECO:0007744|PDB:1XTS, ECO:0007744|PDB:6BCU
ChainResidueDetails
ASER16
BASN119
BASP122
BALA150
AGLY18
AALA35
AASN119
AASP122
AALA150
BSER16
BGLY18
BALA35

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:15728574, ECO:0000269|PubMed:22002721, ECO:0000269|PubMed:22819219, ECO:0000269|PubMed:32470140, ECO:0007744|PDB:1XTQ, ECO:0007744|PDB:3SEA, ECO:0007744|PDB:3T5G, ECO:0007744|PDB:7BTA, ECO:0007744|PDB:7BTC
ChainResidueDetails
AVAL17
BVAL17

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:15728574, ECO:0000269|PubMed:22002721, ECO:0000269|PubMed:29236692, ECO:0007744|PDB:1XTS, ECO:0007744|PDB:6BCU
ChainResidueDetails
ALYS19
BLYS19

site_idSWS_FT_FI4
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:15728574, ECO:0000269|PubMed:29236692, ECO:0000269|PubMed:29416044, ECO:0007744|PDB:5YXH, ECO:0007744|PDB:6BCU, ECO:0007744|PDB:6BSX, ECO:0007744|PDB:6BT0
ChainResidueDetails
ASER20
BSER20

site_idSWS_FT_FI5
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:15728574, ECO:0007744|PDB:1XTS
ChainResidueDetails
ASER21
AVAL32
BSER21
BVAL32

site_idSWS_FT_FI6
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:15728574, ECO:0000269|PubMed:22002721, ECO:0000269|PubMed:22819219, ECO:0000269|PubMed:29416044, ECO:0000269|PubMed:32470140, ECO:0007744|PDB:3SEA, ECO:0007744|PDB:6BT0, ECO:0007744|PDB:7BTA, ECO:0007744|PDB:7BTC
ChainResidueDetails
AASP33
BASP33

site_idSWS_FT_FI7
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:15728574, ECO:0000269|PubMed:29236692, ECO:0007744|PDB:6BCU
ChainResidueDetails
ATHR38
BTHR38

site_idSWS_FT_FI8
Number of Residues2
DetailsSITE: Important for autoinhibition of GTPase activity => ECO:0000269|PubMed:22819219
ChainResidueDetails
AALA35
BALA35

site_idSWS_FT_FI9
Number of Residues2
DetailsMOD_RES: Phosphoserine; by MAPKAPK5 => ECO:0000250|UniProtKB:Q921J2
ChainResidueDetails
ASER130
BSER130

site_idSWS_FT_FI10
Number of Residues4
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:30514904
ChainResidueDetails
ALYS8
BLYS8

218853

PDB entries from 2024-04-24

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