Structure of PDB 7pe8 Chain E Binding Site BS01
Receptor Information
>7pe8 Chain E (length=1115) Species:
9606
(Homo sapiens) [
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NVPLDLTREPSDNLREILQNVARLQGVSNMRKLGHLNNFTKLLCDIGHSE
EKLGFHYEDIIICLRLALLNEAKEVRAAGLRALRYLIQDSSILQKVLKLK
VDYLIARCIDIQQSNEVERTQALRLVRKMITVNASLFPSSVTNSLIAVGN
DGLQERDRMVRACIAIICELALQNPEVVALRGGLNTILKNVIDCQLSRIN
EALITTILHLLNHPKTRQYVRADVELERILAPYTDFHYRHSPDTAEGQLK
EDREARFLASKMGIIATFRSWAGIINLCKPGNSGIQSLIGVLCIPNMEIR
RGLLEVLYDIFRLPLPVVTEEFIEALLSVDPGRFQDSWRLSDGFVAAEAK
TILPHRARSRPDLMDNYLALILSAFIRNGLLEGLVEVITNSDDHISVRAT
ILLGELLHMANTILPHSHSHHLHCLPTLMNMAASFDIPKEKRLRASAALN
CLKRFHEMKKRGPKPYSLHLDHIIQKAIATHQKRDQILKDTEEALLINLR
DSQVLQHKENLEWNWNLIGTILKWPNVNLRNYKDEQLHRFVRRLLYFYKP
SSKLYANLDLDFAKAKQLTVVGCQFTEFLLESEEDGQGYLEDLVKDIVQW
LNASSGMKPERSLQNNGLLTTLSQHYFLFIGTLSCHPHGVKMLEKCSVFQ
CLLNLCSLKNQDHLLKLTVSSLDYSRDGLARVILSKILTAATDACRLYAT
KHLRVLLRANVEFFNNWGIELLVTQLHDKNKTISSEALDILDEACEDKAN
LHALIQMKPALSHLGDKGLLLLLRFLSIPKGFSYLNERGYVAKQLEKWHR
EYNSKYVDLIEEQLNEALTTYRKPQRPHVYLPIHLYGQLVHHKTGCHLLE
VQNIITELCRNVRTPDLDKWEEIKKLKASLWALGNIGSSNWGLNLLQEEN
VIPDILKLAKQCEVLSIRGTCVYVLGLIAKTKQGCDILKCHNWDAVRHSR
KHLWPVVPDYIGLALPVDINDIFQVKDIPYFQTKSFHLLRQQMSLTEIMN
TGLQEHTDDNCLYCVCIEILGFQPSNQMCRILLRKEVLRLVINLSSSVST
KCHETGLLTIKEKYPQTFDDICLYSEVSHLLSHCTFRLPCRRFIQELFQD
VQFLQMHEEAEAVLA
Ligand information
Ligand ID
ZN
InChI
InChI=1S/Zn/q+2
InChIKey
PTFCDOFLOPIGGS-UHFFFAOYSA-N
SMILES
Software
SMILES
CACTVS 3.341
[Zn++]
ACDLabs 10.04
OpenEye OEToolkits 1.5.0
[Zn+2]
Formula
Zn
Name
ZINC ION
ChEMBL
CHEMBL1236970
DrugBank
DB14532
ZINC
PDB chain
7pe8 Chain E Residue 4801 [
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Receptor-Ligand Complex Structure
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PDB
7pe8
Regulation of human mTOR complexes by DEPTOR.
Resolution
3.2 Å
Binding residue
(original residue number in PDB)
H1515 C1520 C1523 C1651
Binding residue
(residue number reindexed from 1)
H1006 C1011 C1014 C1072
Annotation score
4
Enzymatic activity
Enzyme Commision number
?
Gene Ontology
Molecular Function
GO:0005515
protein binding
GO:0019901
protein kinase binding
GO:0043022
ribosome binding
GO:0043539
protein serine/threonine kinase activator activity
GO:0060090
molecular adaptor activity
Biological Process
GO:0001932
regulation of protein phosphorylation
GO:0001938
positive regulation of endothelial cell proliferation
GO:0007010
cytoskeleton organization
GO:0009792
embryo development ending in birth or egg hatching
GO:0010468
regulation of gene expression
GO:0018105
peptidyl-serine phosphorylation
GO:0030036
actin cytoskeleton organization
GO:0030307
positive regulation of cell growth
GO:0030838
positive regulation of actin filament polymerization
GO:0031669
cellular response to nutrient levels
GO:0031929
TOR signaling
GO:0032008
positive regulation of TOR signaling
GO:0032956
regulation of actin cytoskeleton organization
GO:0038203
TORC2 signaling
GO:0043066
negative regulation of apoptotic process
GO:0050727
regulation of inflammatory response
GO:0050731
positive regulation of peptidyl-tyrosine phosphorylation
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:2000114
regulation of establishment of cell polarity
Cellular Component
GO:0005794
Golgi apparatus
GO:0005829
cytosol
GO:0031932
TORC2 complex
View graph for
Molecular Function
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Biological Process
View graph for
Cellular Component
External links
PDB
RCSB:7pe8
,
PDBe:7pe8
,
PDBj:7pe8
PDBsum
7pe8
PubMed
34519268
UniProt
Q6R327
|RICTR_HUMAN Rapamycin-insensitive companion of mTOR (Gene Name=RICTOR)
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