Structure of PDB 1cjk Chain B Binding Site BS01

Receptor Information
>1cjk Chain B (length=190) Species: 10116 (Rattus norvegicus) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
LYHQSYDCVCVMFASIPDFKEFYTESDVNKEGLECLRLLNEIIADFDDLL
SKPKFSGVEKIKTIGSTYMAATGLSARQYMHIGTMVEFAYALVGKLDAIN
KHSFNDFKLRVGINHGPVIAGVIGAQKPQYDIWGNTVNVASRMDSTGVLD
KIQVTEETSLILQTLGYTCTCRGIINVKGKGDLKTYFVNT
Ligand information
Ligand IDTAT
InChIInChI=1S/C10H16N5O12P3S/c11-8-5-9(13-2-12-8)15(3-14-5)10-7(17)6(16)4(25-10)1-24-30(23,31)27-29(21,22)26-28(18,19)20/h2-4,6-7,10,16-17H,1H2,(H,21,22)(H,23,31)(H2,11,12,13)(H2,18,19,20)/t4-,6-,7-,10-,30-/m1/s1
InChIKeyROYJKVPBJVNHCQ-AJBXOXQOSA-N
SMILES
SoftwareSMILES
ACDLabs 12.01O=P(O)(O)OP(=O)(O)OP(=O)(S)OCC3OC(n2cnc1c(ncnc12)N)C(O)C3O
OpenEye OEToolkits 1.7.6c1nc(c2c(n1)n(cn2)C3C(C(C(O3)COP(=O)(OP(=O)(O)OP(=O)(O)O)S)O)O)N
OpenEye OEToolkits 1.7.6c1nc(c2c(n1)n(cn2)[C@H]3[C@@H]([C@@H]([C@H](O3)CO[P@](=O)(OP(=O)(O)OP(=O)(O)O)S)O)O)N
CACTVS 3.370Nc1ncnc2n(cnc12)[C@@H]3O[C@H](CO[P@](S)(=O)O[P](O)(=O)O[P](O)(O)=O)[C@@H](O)[C@H]3O
CACTVS 3.370Nc1ncnc2n(cnc12)[CH]3O[CH](CO[P](S)(=O)O[P](O)(=O)O[P](O)(O)=O)[CH](O)[CH]3O
FormulaC10 H16 N5 O12 P3 S
NameADENOSINE-5'-RP-ALPHA-THIO-TRIPHOSPHATE
ChEMBL
DrugBankDB02355
ZINC
PDB chain1cjk Chain A Residue 801 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
PDB1cjk Two-metal-Ion catalysis in adenylyl cyclase.
Resolution3.0 Å
Binding residue
(original residue number in PDB)		D1018 V1024 N1025 R1029
Binding residue
(residue number reindexed from 1)		D131 V137 N138 R142
Annotation score4
Enzymatic activity
Catalytic site (original residue number in PDB) S891 I892 S942 R1029 K1065
Catalytic site (residue number reindexed from 1) S15 I16 S66 R142 K178
Enzyme Commision number 4.6.1.1: adenylate cyclase.
Gene Ontology
Molecular Function
GO:0016849 phosphorus-oxygen lyase activity
Biological Process
GO:0009190 cyclic nucleotide biosynthetic process
GO:0035556 intracellular signal transduction

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:1cjk, PDBe:1cjk, PDBj:1cjk
PDBsum1cjk
PubMed10427002
UniProtP26769|ADCY2_RAT Adenylate cyclase type 2 (Gene Name=Adcy2)

[Back to BioLiP]