Structure of PDB 6bcu Chain A Binding Site BS01

Receptor Information
>6bcu Chain A (length=2204) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
AAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAATRFYDQLNHHIFELERKG
GILAIASLIGVEGGNATRIGRFANYLRNLLPSNDPVVMEMASKAIGRLAM
AGDTFTAEYVEFEVKRALEWLGADRNEGRRHAAVLVLRELAISVPTFFFQ
QVQPFFDNIFVAVWDPKQAIREGAVAALRACLILTTQREPKEMQKPQWYR
HTFEEAEKGFDDDRIHGALLILNELVRISSMEGERLREEMEEIAAAAAAA
AAAAAAAAAAAAAAAAAASLIQMTILNLLPRLAAFRPTQYLQDTMNHVLS
CVKKEKERTAAFQALGLLSVAVRSEFKVYLPRVLDIIRAALPPKVDATVF
TCISMLARAMGPGIQQDIKELLEPMLAVGLSPALTAVLYDLSRQIPQLKK
DIQDGLLKMLSLVLMAAVGSITLALRTLGSFEFEGHSLTQFVRHCADHFL
NSEHKEIRMEAARTCSRLLTPSVSQTAVQVVADVLSKLLVVGITDPDPDI
RYCVLASLDERFDAHLAQAENLQALFVALNDQVFEIRELAICTVGRLSSM
NPAFVMPFLRKMLIQILTELEHSGIGRIKEQSARMLGHLVSNAPRLIRPY
MEPILKALILKLKDPDPDPNPGVINNVLATIGELAQVSGLEMRKWVDELF
IIIMDMLQDSSLLAKRQVALWTLGQLVASTGYVVEPYRKYPTLLEVLLNF
LKTEQNQGTRREAIRVLGLLGALDPYKHKVNIEMLVNMGNLPLDEFYPAV
SMVALMRIFRDQSLSHHHTMVVQAITFIFKSLGLKCVQFLPQVMPTFLNV
IRVCDGAIREFLFQQLGMLVSFVKSHIRPYMDEIVTLMREFWVMNTSIQS
TIILLIEQIVVALGGEFKLYLPQLIPHMLRVFMHDNSPGRIVSIKLLAAI
QLFGANLDDYLHLLLPPIVKLFDAPEAPLPSRKAALETVDRLTESLDFTD
YASRIIHPIVRTLDQSPELRSTAMDTLSSLVFQLGKKYQIFIPMVNKVLV
RHRINHQRYDVLICRIVKGYTLSTINLQKAWGAARRVSKDDWLEWLRRLS
LELLKDSSSPSLRSCWALAQAYNPMARDLFNAAFVSCWSELNEDQQDELI
RSIELALTSQDIAEVTQTLLNLAEFMEHSDKGPLPLRDDNGIVLLGERAA
KCRAYAKALHYKELEFQKGPTPAILESLISINNKLQQPEAAAGVLEYAMK
HFGELEIQATWYEKLHEWEDALVAYDKKMDTNKDDPELMLGRMRCLEALG
EWGQLHQQCCEKWTLVNDETQAKMARMAAAAAWGLGQWDSMEEYTCMIPR
DTHDGAFYRAVLALHQDLFSLAQQCIDKARDLLDAELTAMAGESYSRAYG
AMVSCHMLSELEEVIQYKLVPERREIIRQIWWERLQGCQRIVEDWQKILM
VRSLVVSPHEDMRTWLKYASLCGKSGRLALAHKTLVLLLGVDPSRQLDHP
LPTVHPQVTYAYMKNMWKSARKIDAFQHMQHFVQTMQQQAQHAIATEDQQ
HKQELHKLMARCFLKLGEWQLNLQGINESTIPKVLQYYSAATEHDRSWYK
AWHAWAVMNFEAVLHYKHQNQARDEKKKVTEDLSKTLLMYTVPAVQGFFR
SISLSRGNNLQDTLRVLTLWFDYGHWPDVNEALVEGVKAIQIDTWLQVIP
QLIARIDTPRPLVGRLIHQLLTDIGRYHPQALIYPLTVASKSTTTARHNA
ANKILKNMCEHSNTLVQQAMMVSEELIRVAILWHEMWHEGLEEASRLYFG
ERNVKGMFEVLEPLHAMMERGPQTLKETSFNQAYGRDLMEAQEWCRKYMK
SGNVKDLTQAWDLYYHVFRRISKQLPQLTSLELQYVSPKLLMCRDLELAV
PGTYDPNQPIIRIQSIAPSLQVITSKQRPRKLTLMGSNGHEFVFLLKGHE
DLRQDERVMQLFGLVNTLLANDPTSLRKNLSIQRYAVIPLSTNSGLIGWV
PHCDTLHALIRDYREKKKILLNIEHRIMLRMAPDYDHLTLMQKVEVFEHA
VNNTAGDDLAKLLWLKSPSSEVWFDRRTNYTRSLAVMSMVGYILGLGDRH
PSNLMLDRLSGKILHIDFGDCFEVAMTREKFPEKIPFRLTRMLTNAMEVT
GLDGNYRITCHTVMEVLREHKDSVMAVLEAFVYDPLLNWRLMDTNTALNK
KAIQIINRVRDKLTGRDFSHDDTLDVPTQVELLIKQATSHENLCQCYIGW
CPFW
Ligand information
Ligand IDATP
InChIInChI=1S/C10H16N5O13P3/c11-8-5-9(13-2-12-8)15(3-14-5)10-7(17)6(16)4(26-10)1-25-30(21,22)28-31(23,24)27-29(18,19)20/h2-4,6-7,10,16-17H,1H2,(H,21,22)(H,23,24)(H2,11,12,13)(H2,18,19,20)/t4-,6-,7-,10-/m1/s1
InChIKeyZKHQWZAMYRWXGA-KQYNXXCUSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.5.0c1nc(c2c(n1)n(cn2)C3C(C(C(O3)COP(=O)(O)OP(=O)(O)OP(=O)(O)O)O)O)N
CACTVS 3.341Nc1ncnc2n(cnc12)[CH]3O[CH](CO[P](O)(=O)O[P](O)(=O)O[P](O)(O)=O)[CH](O)[CH]3O
ACDLabs 10.04O=P(O)(O)OP(=O)(O)OP(=O)(O)OCC3OC(n2cnc1c(ncnc12)N)C(O)C3O
OpenEye OEToolkits 1.5.0c1nc(c2c(n1)n(cn2)[C@H]3[C@@H]([C@@H]([C@H](O3)CO[P@@](=O)(O)O[P@](=O)(O)OP(=O)(O)O)O)O)N
CACTVS 3.341Nc1ncnc2n(cnc12)[C@@H]3O[C@H](CO[P@](O)(=O)O[P@@](O)(=O)O[P](O)(O)=O)[C@@H](O)[C@H]3O
FormulaC10 H16 N5 O13 P3
NameADENOSINE-5'-TRIPHOSPHATE
ChEMBLCHEMBL14249
DrugBankDB00171
ZINCZINC000004261765
PDB chain6bcu Chain A Residue 3000 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

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PDB6bcu Mechanisms of mTORC1 activation by RHEB and inhibition by PRAS40.
Resolution3.8 Å
Binding residue
(original residue number in PDB)		K2166 Q2167 K2187 Y2225 V2240 M2345 I2356
Binding residue
(residue number reindexed from 1)		K1876 Q1877 K1897 Y1935 V1950 M2055 I2066
Annotation score5
Enzymatic activity
Enzyme Commision number 2.7.11.1: non-specific serine/threonine protein kinase.
Gene Ontology
Molecular Function
GO:0001002 RNA polymerase III type 1 promoter sequence-specific DNA binding
GO:0001003 RNA polymerase III type 2 promoter sequence-specific DNA binding
GO:0001006 RNA polymerase III type 3 promoter sequence-specific DNA binding
GO:0001156 TFIIIC-class transcription factor complex binding
GO:0004672 protein kinase activity
GO:0004674 protein serine/threonine kinase activity
GO:0005515 protein binding
GO:0005524 ATP binding
GO:0016301 kinase activity
GO:0042802 identical protein binding
GO:0043022 ribosome binding
GO:0044024 histone H2AS1 kinase activity
GO:0044877 protein-containing complex binding
GO:0051219 phosphoprotein binding
GO:0106310 protein serine kinase activity
Biological Process
GO:0001558 regulation of cell growth
GO:0002296 T-helper 1 cell lineage commitment
GO:0003007 heart morphogenesis
GO:0003179 heart valve morphogenesis
GO:0006112 energy reserve metabolic process
GO:0006207 'de novo' pyrimidine nucleobase biosynthetic process
GO:0006338 chromatin remodeling
GO:0006468 protein phosphorylation
GO:0006954 inflammatory response
GO:0006974 DNA damage response
GO:0007010 cytoskeleton organization
GO:0007040 lysosome organization
GO:0007281 germ cell development
GO:0007584 response to nutrient
GO:0008361 regulation of cell size
GO:0009267 cellular response to starvation
GO:0009408 response to heat
GO:0009791 post-embryonic development
GO:0010506 regulation of autophagy
GO:0010507 negative regulation of autophagy
GO:0010592 positive regulation of lamellipodium assembly
GO:0010628 positive regulation of gene expression
GO:0010718 positive regulation of epithelial to mesenchymal transition
GO:0010831 positive regulation of myotube differentiation
GO:0016236 macroautophagy
GO:0016241 regulation of macroautophagy
GO:0016242 negative regulation of macroautophagy
GO:0016310 phosphorylation
GO:0018105 peptidyl-serine phosphorylation
GO:0019219 regulation of nucleobase-containing compound metabolic process
GO:0019228 neuronal action potential
GO:0030030 cell projection organization
GO:0030163 protein catabolic process
GO:0030307 positive regulation of cell growth
GO:0030838 positive regulation of actin filament polymerization
GO:0031295 T cell costimulation
GO:0031529 ruffle organization
GO:0031641 regulation of myelination
GO:0031648 protein destabilization
GO:0031667 response to nutrient levels
GO:0031669 cellular response to nutrient levels
GO:0031670 cellular response to nutrient
GO:0031929 TOR signaling
GO:0032868 response to insulin
GO:0032869 cellular response to insulin stimulus
GO:0032956 regulation of actin cytoskeleton organization
GO:0033173 calcineurin-NFAT signaling cascade
GO:0034198 cellular response to amino acid starvation
GO:0035264 multicellular organism growth
GO:0038202 TORC1 signaling
GO:0042752 regulation of circadian rhythm
GO:0043066 negative regulation of apoptotic process
GO:0043200 response to amino acid
GO:0043276 anoikis
GO:0045670 regulation of osteoclast differentiation
GO:0045727 positive regulation of translation
GO:0045792 negative regulation of cell size
GO:0045821 positive regulation of glycolytic process
GO:0045945 positive regulation of transcription by RNA polymerase III
GO:0045948 positive regulation of translational initiation
GO:0046777 protein autophosphorylation
GO:0046889 positive regulation of lipid biosynthetic process
GO:0048266 behavioral response to pain
GO:0048511 rhythmic process
GO:0048709 oligodendrocyte differentiation
GO:0048714 positive regulation of oligodendrocyte differentiation
GO:0048738 cardiac muscle tissue development
GO:0050731 positive regulation of peptidyl-tyrosine phosphorylation
GO:0050882 voluntary musculoskeletal movement
GO:0051128 regulation of cellular component organization
GO:0051247 positive regulation of protein metabolic process
GO:0051496 positive regulation of stress fiber assembly
GO:0051549 positive regulation of keratinocyte migration
GO:0051647 nucleus localization
GO:0051896 regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction
GO:0051897 positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction
GO:0055006 cardiac cell development
GO:0055013 cardiac muscle cell development
GO:0060048 cardiac muscle contraction
GO:0061431 cellular response to methionine
GO:0070885 negative regulation of calcineurin-NFAT signaling cascade
GO:0071230 cellular response to amino acid stimulus
GO:0071233 cellular response to L-leucine
GO:0071456 cellular response to hypoxia
GO:0071470 cellular response to osmotic stress
GO:0080135 regulation of cellular response to stress
GO:0090559 regulation of membrane permeability
GO:1900034 regulation of cellular response to heat
GO:1900181 negative regulation of protein localization to nucleus
GO:1901796 regulation of signal transduction by p53 class mediator
GO:1901838 positive regulation of transcription of nucleolar large rRNA by RNA polymerase I
GO:1903691 positive regulation of wound healing, spreading of epidermal cells
GO:1904059 regulation of locomotor rhythm
GO:1904690 positive regulation of cytoplasmic translational initiation
GO:1905672 negative regulation of lysosome organization
GO:1905857 positive regulation of pentose-phosphate shunt
GO:1990253 cellular response to leucine starvation
GO:2000785 regulation of autophagosome assembly
Cellular Component
GO:0000139 Golgi membrane
GO:0005634 nucleus
GO:0005635 nuclear envelope
GO:0005654 nucleoplasm
GO:0005737 cytoplasm
GO:0005739 mitochondrion
GO:0005741 mitochondrial outer membrane
GO:0005764 lysosome
GO:0005765 lysosomal membrane
GO:0005783 endoplasmic reticulum
GO:0005789 endoplasmic reticulum membrane
GO:0005794 Golgi apparatus
GO:0005829 cytosol
GO:0012505 endomembrane system
GO:0016020 membrane
GO:0016605 PML body
GO:0030425 dendrite
GO:0031410 cytoplasmic vesicle
GO:0031931 TORC1 complex
GO:0031932 TORC2 complex
GO:0045335 phagocytic vesicle

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Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:6bcu, PDBe:6bcu, PDBj:6bcu
PDBsum6bcu
PubMed29236692
UniProtP42345|MTOR_HUMAN Serine/threonine-protein kinase mTOR (Gene Name=MTOR)

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