Structure of PDB 3r7w Chain D

Receptor sequence
>3r7wD (length=229) Species: 4932 (Saccharomyces cerevisiae) [Search protein sequence]
MVLLMGVRRCGKSSICKVVFHALVYVIDINAITNLAMIIEYAYKVNPSIN
IEVLIHKFKVDAQRDIMQRTGEELLELGLDGVQVSFYLTSIFDHSIYEAF
SRIVQKLIPELSFLENMLDNLIQHSKIEKAFLFDVNSKIYVSTDSNPVDI
QMYEVCSEFIDVTIDLFDLYKAELQNVSQLANGVIIYLRQMIRGLALVAI
IRPNGTDMESCLTVADYNIDIFKKGLEDI
3D structure
PDB3r7w Crystal structure of the Gtr1p-Gtr2p complex reveals new insights into the amino acid-induced TORC1 activation
ChainD
Resolution2.773 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 3.6.5.-
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 GNP D C20 K22 S24 H124 K125 I166 C10 K12 S14 H56 K57 I91
Gene Ontology
Molecular Function
GO:0003924 GTPase activity
GO:0005515 protein binding
GO:0005525 GTP binding
GO:0016787 hydrolase activity
Biological Process
GO:0006995 cellular response to nitrogen starvation
GO:0009267 cellular response to starvation
GO:0010507 negative regulation of autophagy
GO:0016237 microautophagy
GO:0032008 positive regulation of TOR signaling
GO:0032456 endocytic recycling
GO:0034599 cellular response to oxidative stress
GO:0045944 positive regulation of transcription by RNA polymerase II
GO:0071230 cellular response to amino acid stimulus
GO:1903778 protein localization to vacuolar membrane
GO:1904263 positive regulation of TORC1 signaling
Cellular Component
GO:0000329 fungal-type vacuole membrane
GO:0000785 chromatin
GO:0005634 nucleus
GO:0005737 cytoplasm
GO:0005770 late endosome
GO:0005773 vacuole
GO:0005774 vacuolar membrane
GO:0016020 membrane
GO:0031902 late endosome membrane
GO:0045121 membrane raft
GO:0071986 Ragulator complex
GO:1990131 Gtr1-Gtr2 GTPase complex

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Cellular Component
External links
PDB RCSB:3r7w, PDBe:3r7w, PDBj:3r7w
PDBsum3r7w
PubMed21816923
UniProtP53290|RAGCD_YEAST GTP-binding protein GTR2 (Gene Name=GTR2)

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