Structure of PDB 1tl7 Chain C Binding Site BS01

Receptor Information
>1tl7 Chain C (length=330) Species: 9913 (Bos taurus) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
ATHRLLLLGAGESGKSTIVKQMRILHVGEKATKVQDIKNNLKEAIETIVA
AMSNLVPPVELANPENQFRVDYILSVMNVPDFDFPPEFYEHAKALWEDEG
VRACYERSNEYQLIDCAQYFLDKIDVIKQDDYVPSDQDLLRCRVLTSGIF
ETKFQVDKVNFHMFDVGGQRDERRKWIQCFNDVTAIIFVVASSSYNMVIR
EDNQTNRLQEALNLFKSIWNNRWLRTISVILFLNKQDLLAEKVLAGKSKI
EDYFPEFARYTTPEDATPEPGEDPRVTRAKYFIRDEFLRISTASGDGRHY
CYPHFTCAVDTENIRRVFNDCRDIIQRMHL
Ligand information
Ligand IDMG
InChIInChI=1S/Mg/q+2
InChIKeyJLVVSXFLKOJNIY-UHFFFAOYSA-N
SMILES
SoftwareSMILES
ACDLabs 10.04
OpenEye OEToolkits 1.5.0		[Mg+2]
CACTVS 3.341[Mg++]
FormulaMg
NameMAGNESIUM ION
ChEMBL
DrugBankDB01378
ZINC
PDB chain1tl7 Chain C Residue 403 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB1tl7 Structural basis for the inhibition of mammalian membrane adenylyl cyclase by 2 '(3')-O-(N-Methylanthraniloyl)-guanosine 5 '-triphosphate.
Resolution2.8 Å
Binding residue
(original residue number in PDB)		S54 T204
Binding residue
(residue number reindexed from 1)		S16 T146
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) E50 T55 R201 D223 Q227
Catalytic site (residue number reindexed from 1) E12 T17 R143 D165 Q169
Enzyme Commision number ?
Gene Ontology
Molecular Function
GO:0003924 GTPase activity
GO:0005525 GTP binding
GO:0019001 guanyl nucleotide binding
GO:0031683 G-protein beta/gamma-subunit complex binding
Biological Process
GO:0007165 signal transduction
GO:0007186 G protein-coupled receptor signaling pathway

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Molecular Function
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Biological Process
External links
PDB RCSB:1tl7, PDBe:1tl7, PDBj:1tl7
PDBsum1tl7
PubMed15591060
UniProtP04896|GNAS2_BOVIN Guanine nucleotide-binding protein G(s) subunit alpha isoforms short (Gene Name=GNAS)

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