Structure of PDB 6bcx Chain W Binding Site BS01
Receptor Information
>6bcx Chain W (length=1052) Species:
9606
(Homo sapiens) [
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EADLTDWNLPLAFMKKRHCEKIEGSKSLAQSWRMKDRMKTVSVALVLCLN
VGVDPPDVVKTTPCARLECWIDPLSMGPQKALETIGANLQKQYENWQPRA
RYKQSLDPTVDEVKKLCTSLRRNAKEERVLFHYNGHGVPRPTVNGEVWVF
NKNYTQYIPLSIYDLQTWMGSPSIFVYDCSNAGLIVKSFKQFALQREQEL
EVSMKNCIQLAACEATELLPMIPDLPADLFTSCLTTPIKIALRWFCMQKC
VSLVPGVTLDLIEKIPGRLNDRRTPLGELNWIFTAITDTIAWNVLPRDLF
QKLFRQDLLVASLFRNFLLAERIMRSYNCTPVSSPRLPPTYMHAMWQAWD
LAVDICLSQLPTIIEEGTAFRHSPFFAEQLTAFQVWLTMGVENRNPPEQL
PIVLQVLLSQVHRLRALDLLGRFLDLGPWAVSLALSVGIFPYVLKLLQSS
ARELRPLLVFIWAKILAVDSSCQADLVKDNGHKYFLSVLADPYMPAEHRT
MTAFILAVIVNSYHTGQEACLQGNLIAICLEQLNDPHPLLRQWVAICLGR
IWQNFDSARWCGVRDSAHEKLYSLLSDPIPEVRCAAVFALGTFVGNSAER
TDHSTTIDHNVAMMLAQLVSDGSPMVRKELVVALSHLVVQYESNFCTVAL
QFISVYTQIWRVLLHLAADPYPEVSDVAMKVLNSIAYKFISATVQTGFCD
WSARYFAQPVMKIPEEHDLESQIRKEREWRFLRNSRVRRQAQQVIQKGIT
RLDDQIFLNRNPGVPSVVKFHPFTPCIAVADKDSICFWDWEKGEKLDYFH
NGNPRYTRVTAMEYLNGQDCSLLLTATDDGAIRVWKNFADLEKNPEMVTA
WQGLSAGMVVDWEQETGLLMSSGDVRIVRIWDTDREMKVQDIPTGADSCV
TSLSCDSHRSLIVAGLGDGSIRVYDRRMALSECRVMTYREHTAWVVKASL
QKRPDGHIVSVSVNGDVRIFDPRMPESVNVLQIVKGLTALDIHPQADLIA
CGSVNQFTAIYNSSGELINNIKYAISCLAFHPHWPHLAVGSNDYYISVYS
VE
Ligand information
>6bcx Chain X (length=8) Species:
9606
(Homo sapiens) [
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ESQFEMDI
Receptor-Ligand Complex Structure
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PDB
6bcx
Mechanisms of mTORC1 activation by RHEB and inhibition by PRAS40.
Resolution
3.23 Å
Binding residue
(original residue number in PDB)
R305 F337 R338 L341 Q438 L441 R446 Y475 K478
Binding residue
(residue number reindexed from 1)
R272 F304 R305 L308 Q405 L408 R413 Y442 K445
Enzymatic activity
Enzyme Commision number
?
Gene Ontology
Molecular Function
GO:0005515
protein binding
GO:0019901
protein kinase binding
GO:0030291
protein serine/threonine kinase inhibitor activity
GO:0030295
protein kinase activator activity
GO:0030674
protein-macromolecule adaptor activity
GO:0031267
small GTPase binding
GO:0044877
protein-containing complex binding
GO:0071889
14-3-3 protein binding
GO:0140767
enzyme-substrate adaptor activity
Biological Process
GO:0001558
regulation of cell growth
GO:0001938
positive regulation of endothelial cell proliferation
GO:0006974
DNA damage response
GO:0008361
regulation of cell size
GO:0009267
cellular response to starvation
GO:0009410
response to xenobiotic stimulus
GO:0010506
regulation of autophagy
GO:0010507
negative regulation of autophagy
GO:0010800
positive regulation of peptidyl-threonine phosphorylation
GO:0030307
positive regulation of cell growth
GO:0031669
cellular response to nutrient levels
GO:0031929
TOR signaling
GO:0032008
positive regulation of TOR signaling
GO:0033138
positive regulation of peptidyl-serine phosphorylation
GO:0035176
social behavior
GO:0038202
TORC1 signaling
GO:0045672
positive regulation of osteoclast differentiation
GO:0045821
positive regulation of glycolytic process
GO:0045945
positive regulation of transcription by RNA polymerase III
GO:0046889
positive regulation of lipid biosynthetic process
GO:0071230
cellular response to amino acid stimulus
GO:0071233
cellular response to L-leucine
GO:0071333
cellular response to glucose stimulus
GO:0071456
cellular response to hypoxia
GO:0071470
cellular response to osmotic stress
GO:1900087
positive regulation of G1/S transition of mitotic cell cycle
GO:1901331
positive regulation of odontoblast differentiation
GO:1905857
positive regulation of pentose-phosphate shunt
Cellular Component
GO:0005654
nucleoplasm
GO:0005737
cytoplasm
GO:0005764
lysosome
GO:0005765
lysosomal membrane
GO:0005829
cytosol
GO:0010494
cytoplasmic stress granule
GO:0016020
membrane
GO:0030425
dendrite
GO:0031931
TORC1 complex
GO:0043025
neuronal cell body
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Molecular Function
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Biological Process
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Cellular Component
External links
PDB
RCSB:6bcx
,
PDBe:6bcx
,
PDBj:6bcx
PDBsum
6bcx
PubMed
29236692
UniProt
Q8N122
|RPTOR_HUMAN Regulatory-associated protein of mTOR (Gene Name=RPTOR)
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