Structure of PDB 6bcx Chain Y

Receptor sequence

>6bcxY (length=1052) Species: 9606 (Homo sapiens)

EADLTDWNLPLAFMKKRHCEKIEGSKSLAQSWRMKDRMKTVSVALVLCLN
VGVDPPDVVKTTPCARLECWIDPLSMGPQKALETIGANLQKQYENWQPRA
RYKQSLDPTVDEVKKLCTSLRRNAKEERVLFHYNGHGVPRPTVNGEVWVF
NKNYTQYIPLSIYDLQTWMGSPSIFVYDCSNAGLIVKSFKQFALQREQEL
EVSMKNCIQLAACEATELLPMIPDLPADLFTSCLTTPIKIALRWFCMQKC
VSLVPGVTLDLIEKIPGRLNDRRTPLGELNWIFTAITDTIAWNVLPRDLF
QKLFRQDLLVASLFRNFLLAERIMRSYNCTPVSSPRLPPTYMHAMWQAWD
LAVDICLSQLPTIIEEGTAFRHSPFFAEQLTAFQVWLTMGVENRNPPEQL
PIVLQVLLSQVHRLRALDLLGRFLDLGPWAVSLALSVGIFPYVLKLLQSS
ARELRPLLVFIWAKILAVDSSCQADLVKDNGHKYFLSVLADPYMPAEHRT
MTAFILAVIVNSYHTGQEACLQGNLIAICLEQLNDPHPLLRQWVAICLGR
IWQNFDSARWCGVRDSAHEKLYSLLSDPIPEVRCAAVFALGTFVGNSAER
TDHSTTIDHNVAMMLAQLVSDGSPMVRKELVVALSHLVVQYESNFCTVAL
QFISVYTQIWRVLLHLAADPYPEVSDVAMKVLNSIAYKFISATVQTGFCD
WSARYFAQPVMKIPEEHDLESQIRKEREWRFLRNSRVRRQAQQVIQKGIT
RLDDQIFLNRNPGVPSVVKFHPFTPCIAVADKDSICFWDWEKGEKLDYFH
NGNPRYTRVTAMEYLNGQDCSLLLTATDDGAIRVWKNFADLEKNPEMVTA
WQGLSAGMVVDWEQETGLLMSSGDVRIVRIWDTDREMKVQDIPTGADSCV
TSLSCDSHRSLIVAGLGDGSIRVYDRRMALSECRVMTYREHTAWVVKASL
QKRPDGHIVSVSVNGDVRIFDPRMPESVNVLQIVKGLTALDIHPQADLIA
CGSVNQFTAIYNSSGELINNIKYAISCLAFHPHWPHLAVGSNDYYISVYS
VE

3D structure

• PDB: 6bcx Mechanisms of mTORC1 activation by RHEB and inhibition by PRAS40.
• Chain: Y
• Resolution: 3.23 Å

Interaction with ligand

Site #	Ligand	Ligand chain	Binding residues on receptor (original residue number in PDB)	Binding residues on receptor (residue number reindexed from 1)	Binding affinity
BS01	peptide	Y	R305 F337 R338 L341 Q438 L441 R446 Y475 K478	R272 F304 R305 L308 Q405 L408 R413 Y442 K445

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

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)