Structure of PDB 1cjt Chain C Binding Site BS02

Receptor Information
>1cjt 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 IDGSP
InChIInChI=1S/C10H16N5O13P3S/c11-10-13-7-4(8(18)14-10)12-2-15(7)9-6(17)5(16)3(26-9)1-25-29(19,20)27-30(21,22)28-31(23,24)32/h2-3,5-6,9,16-17H,1H2,(H,19,20)(H,21,22)(H2,23,24,32)(H3,11,13,14,18)/t3-,5-,6-,9-/m1/s1
InChIKeyXOFLBQFBSOEHOG-UUOKFMHZSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.5.0c1nc2c(n1C3C(C(C(O3)COP(=O)(O)OP(=O)(O)OP(=S)(O)O)O)O)N=C(NC2=O)N
CACTVS 3.341NC1=Nc2n(cnc2C(=O)N1)[C@@H]3O[C@H](CO[P@@](O)(=O)O[P@@](O)(=O)O[P](O)(O)=S)[C@@H](O)[C@H]3O
OpenEye OEToolkits 1.5.0c1nc2c(n1[C@H]3[C@@H]([C@@H]([C@H](O3)CO[P@](=O)(O)O[P@](=O)(O)OP(=S)(O)O)O)O)N=C(NC2=O)N
CACTVS 3.341NC1=Nc2n(cnc2C(=O)N1)[CH]3O[CH](CO[P](O)(=O)O[P](O)(=O)O[P](O)(O)=S)[CH](O)[CH]3O
ACDLabs 10.04S=P(O)(O)OP(=O)(O)OP(=O)(O)OCC3OC(n2cnc1c2N=C(N)NC1=O)C(O)C3O
FormulaC10 H16 N5 O13 P3 S
Name5'-GUANOSINE-DIPHOSPHATE-MONOTHIOPHOSPHATE
ChEMBLCHEMBL1204628
DrugBankDB01864
ZINCZINC000008217391
PDB chain1cjt Chain C Residue 405 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB1cjt Two-metal-Ion catalysis in adenylyl cyclase.
Resolution2.8 Å
Binding residue
(original residue number in PDB)		G49 E50 S51 G52 K53 S54 T55 D173 L198 R199 T204 G226 N292 K293 D295 L296 C365 A366 V367
Binding residue
(residue number reindexed from 1)		G11 E12 S13 G14 K15 S16 T17 D115 L140 R141 T146 G168 N234 K235 D237 L238 C307 A308 V309
Annotation score3
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
View graph for
Biological Process
External links
PDB RCSB:1cjt, PDBe:1cjt, PDBj:1cjt
PDBsum1cjt
PubMed10427002
UniProtP04896|GNAS2_BOVIN Guanine nucleotide-binding protein G(s) subunit alpha isoforms short (Gene Name=GNAS)

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