Structure of PDB 1tl7 Chain C

Receptor sequence
>1tl7C (length=330) Species: 9913 (Bos taurus) [Search protein sequence]
ATHRLLLLGAGESGKSTIVKQMRILHVGEKATKVQDIKNNLKEAIETIVA
AMSNLVPPVELANPENQFRVDYILSVMNVPDFDFPPEFYEHAKALWEDEG
VRACYERSNEYQLIDCAQYFLDKIDVIKQDDYVPSDQDLLRCRVLTSGIF
ETKFQVDKVNFHMFDVGGQRDERRKWIQCFNDVTAIIFVVASSSYNMVIR
EDNQTNRLQEALNLFKSIWNNRWLRTISVILFLNKQDLLAEKVLAGKSKI
EDYFPEFARYTTPEDATPEPGEDPRVTRAKYFIRDEFLRISTASGDGRHY
CYPHFTCAVDTENIRRVFNDCRDIIQRMHL
3D structure
PDB1tl7 Structural basis for the inhibition of mammalian membrane adenylyl cyclase by 2 '(3')-O-(N-Methylanthraniloyl)-guanosine 5 '-triphosphate.
ChainC
Resolution2.8 Å
3D
structure
Catalytic site residues are labeled in the structure
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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 ?
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 MG C S54 T204 S16 T146
BS02 GSP C E50 S51 G52 K53 S54 T55 D173 L198 R199 R201 L203 N292 K293 D295 L296 C365 A366 V367 E12 S13 G14 K15 S16 T17 D115 L140 R141 R143 L145 N234 K235 D237 L238 C307 A308 V309
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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