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7BTD

Crystal structure of Rheb Y35N mutant bound to GppNHp

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
Functional Information from PDB Data
site_idAC1
Number of Residues5
Detailsbinding site for residue MG A 201
ChainResidue
ASER20
ATHR38
AGNP202
AHOH319
AHOH321

site_idAC2
Number of Residues26
Detailsbinding site for residue GNP A 202
ChainResidue
ALYS19
ASER20
ASER21
APHE31
AVAL32
AASP33
AASN35
APRO37
ATHR38
AGLY63
AASN119
ALYS120
AASP122
ALEU123
ASER149
AALA150
AMG201
AHOH301
AHOH319
AHOH321
AHOH366
AHOH372
AARG15
ASER16
AVAL17
AGLY18

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
AASN35
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
AASN35

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

site_idSWS_FT_FI10
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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