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3T5G

Structure of fully modified farnesylated Rheb in complex with PDE6D

Functional Information from GO Data
ChainGOidnamespacecontents
A0000139cellular_componentGolgi membrane
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
B0005095molecular_functionGTPase inhibitor activity
B0005515molecular_functionprotein binding
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0005856cellular_componentcytoskeleton
B0005929cellular_componentcilium
B0007601biological_processvisual perception
B0016020cellular_componentmembrane
B0030659cellular_componentcytoplasmic vesicle membrane
B0031267molecular_functionsmall GTPase binding
B0031410cellular_componentcytoplasmic vesicle
B0042995cellular_componentcell projection
B0050953biological_processsensory perception of light stimulus
Functional Information from PDB Data
site_idAC1
Number of Residues25
DetailsBINDING SITE FOR RESIDUE GDP A 201
ChainResidue
ASER16
AASP122
ALEU123
ASER149
AALA150
ALYS151
AHOH197
AMG202
AHOH212
AHOH288
AHOH294
AVAL17
AHOH298
AHOH304
AHOH362
AHOH395
AHOH434
AHOH449
AGLY18
ALYS19
ASER20
ASER21
APHE31
AASN119
ALYS120

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG A 202
ChainResidue
ASER20
AGDP201
AHOH395
AHOH396
AHOH434
AHOH449

site_idAC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE FAR A 2010
ChainResidue
ASER180
ACMT181
BMET20
BLEU38
BILE53
BGLN78
BTYR149

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:15728574, ECO:0000269|PubMed:29236692, ECO:0007744|PDB:1XTS, ECO:0007744|PDB:6BCU
ChainResidueDetails
ASER16
AGLY18
ATYR35
AASN119
AASP122
AALA150

site_idSWS_FT_FI2
Number of Residues1
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

site_idSWS_FT_FI3
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:15728574, ECO:0000269|PubMed:22002721, ECO:0000269|PubMed:29236692, ECO:0007744|PDB:1XTS, ECO:0007744|PDB:6BCU
ChainResidueDetails
ALYS19

site_idSWS_FT_FI4
Number of Residues1
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

site_idSWS_FT_FI5
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:15728574, ECO:0007744|PDB:1XTS
ChainResidueDetails
ASER21
AVAL32

site_idSWS_FT_FI6
Number of Residues1
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

site_idSWS_FT_FI7
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:15728574, ECO:0000269|PubMed:29236692, ECO:0007744|PDB:6BCU
ChainResidueDetails
ATHR38

site_idSWS_FT_FI8
Number of Residues1
DetailsSITE: Important for autoinhibition of GTPase activity => ECO:0000269|PubMed:22819219
ChainResidueDetails
ATYR35

site_idSWS_FT_FI9
Number of Residues1
DetailsMOD_RES: Phosphoserine; by MAPKAPK5 => ECO:0000250|UniProtKB:Q921J2
ChainResidueDetails
ASER130

site_idSWS_FT_FI10
Number of Residues1
DetailsMOD_RES: Cysteine methyl ester => ECO:0000269|PubMed:12906785, ECO:0000269|PubMed:15308774, ECO:0000269|PubMed:22002721, ECO:0007744|PDB:3T5G
ChainResidueDetails
ACMT181

site_idSWS_FT_FI11
Number of Residues1
DetailsLIPID: S-farnesyl cysteine => ECO:0000269|PubMed:12906785, ECO:0000269|PubMed:15308774, ECO:0000269|PubMed:22002721, ECO:0007744|PDB:3T5G
ChainResidueDetails
ACMT181

site_idSWS_FT_FI12
Number of Residues2
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:30514904
ChainResidueDetails
ALYS8

222415

PDB entries from 2024-07-10

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