Structure of PDB 2rio Chain A Binding Site BS02

Receptor Information
>2rio Chain A (length=396) Species: 4932 (Saccharomyces cerevisiae) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
NFEQSLKNLVVSEKILGYGSSGTVVFQGSFQGRPVAVKRMLIDFCDIALM
EIKLLTESDDHPNVIRYYCSETTDRFLYIALELCNLNLQDLVESKYNPIS
LLRQIASGVAHLHSLKIIHRDLKPQNILVSTSSRFTADQQTGAENLRILI
SDFGLCKKLDSTSGWRAPELLEESNNLQTKRRLTRSIDIFSMGCVFYYIL
SKGKHPFGDKYSRESNIIRGIFSLDEMKCLHDRSLIAEATDLISQMIDHD
PLKRPTAMKVLRHPLFWPKSKKLEFLLKVSDRLEIENRDPPSALLMKFDA
GSDFVIPSGDWTVKFDKTFMDRKYHSSKLMDLLRALRNKYHHFMDLPEDI
AELMGPVPDGFYDYFTKRFPNLLIGVYMIVKENLSDDQILREFLYS
Ligand information
Ligand IDADP
InChIInChI=1S/C10H15N5O10P2/c11-8-5-9(13-2-12-8)15(3-14-5)10-7(17)6(16)4(24-10)1-23-27(21,22)25-26(18,19)20/h2-4,6-7,10,16-17H,1H2,(H,21,22)(H2,11,12,13)(H2,18,19,20)/t4-,6-,7-,10-/m1/s1
InChIKeyXTWYTFMLZFPYCI-KQYNXXCUSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.5.0c1nc(c2c(n1)n(cn2)[C@H]3[C@@H]([C@@H]([C@H](O3)CO[P@](=O)(O)OP(=O)(O)O)O)O)N
CACTVS 3.341Nc1ncnc2n(cnc12)[CH]3O[CH](CO[P](O)(=O)O[P](O)(O)=O)[CH](O)[CH]3O
ACDLabs 10.04O=P(O)(O)OP(=O)(O)OCC3OC(n2cnc1c(ncnc12)N)C(O)C3O
CACTVS 3.341Nc1ncnc2n(cnc12)[C@@H]3O[C@H](CO[P@@](O)(=O)O[P](O)(O)=O)[C@@H](O)[C@H]3O
OpenEye OEToolkits 1.5.0c1nc(c2c(n1)n(cn2)C3C(C(C(O3)COP(=O)(O)OP(=O)(O)O)O)O)N
FormulaC10 H15 N5 O10 P2
NameADENOSINE-5'-DIPHOSPHATE
ChEMBLCHEMBL14830
DrugBankDB16833
ZINCZINC000012360703
PDB chain2rio Chain A Residue 1101 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

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PDB2rio Structure of the dual enzyme ire1 reveals the basis for catalysis and regulation in nonconventional RNA splicing.
Resolution2.4 Å
Binding residue
(original residue number in PDB)		Y25 G26 V32 A43 K45 E89 C91 N94 L147 D171
Binding residue
(residue number reindexed from 1)		Y18 G19 V25 A36 K38 E82 C84 N87 L128 D152
Annotation score5
Binding affinityPDBbind-CN: -logKd/Ki=4.69,Kd=20.4uM
Enzymatic activity
Catalytic site (original residue number in PDB) D140 K142 N145 D171 T195
Catalytic site (residue number reindexed from 1) D121 K123 N126 D152 T162
Enzyme Commision number 2.7.11.1: non-specific serine/threonine protein kinase.
3.1.26.-
Gene Ontology
Molecular Function
GO:0004521 RNA endonuclease activity
GO:0004540 RNA nuclease activity
GO:0004672 protein kinase activity
GO:0004674 protein serine/threonine kinase activity
GO:0005524 ATP binding
Biological Process
GO:0006397 mRNA processing
GO:0006468 protein phosphorylation
GO:0030968 endoplasmic reticulum unfolded protein response

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:2rio, PDBe:2rio, PDBj:2rio
PDBsum2rio
PubMed18191223
UniProtP32361|IRE1_YEAST Serine/threonine-protein kinase/endoribonuclease IRE1 (Gene Name=IRE1)

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