Structure of PDB 2rio Chain B

Receptor sequence
>2rioB (length=395) Species: 4932 (Saccharomyces cerevisiae) [Search protein sequence]
NFEQSLKNLVVSEKILGYGSSGTVVFQGSFQGRPVAVKRMLIDFCDIALM
EIKLLTESDDHPNVIRYYCSETTDRFLYIALELCNLNLQDLVESYNPISL
LRQIASGVAHLHSLKIIHRDLKPQNILVSTSSRFTADQQTGAENLRILIS
DFGLCKKLDSTSGWRAPELLEESNNLQTKRRLTRSIDIFSMGCVFYYILS
KGKHPFGDKYSRESNIIRGIFSLDEMKCLHDRSLIAEATDLISQMIDHDP
LKRPTAMKVLRHPLFWPKSKKLEFLLKVSDRLEIENRDPPSALLMKFDAG
SDFVIPSGDWTVKFDKTFMDRKYHSSKLMDLLRALRNKYHHFMDLPEDIA
ELMGPVPDGFYDYFTKRFPNLLIGVYMIVKENLSDDQILREFLYS
3D structure
PDB2rio Structure of the dual enzyme ire1 reveals the basis for catalysis and regulation in nonconventional RNA splicing.
ChainB
Resolution2.4 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D140 K142 N145 D171 T195
Catalytic site (residue number reindexed from 1) D120 K122 N125 D151 T161
Enzyme Commision number 2.7.11.1: non-specific serine/threonine protein kinase.
3.1.26.-
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 B N145 D171 N125 D151
BS02 ADP B G24 Y25 G26 T30 V32 A43 K45 E89 C91 N94 L147 D171 G17 Y18 G19 T23 V25 A36 K38 E82 C84 N87 L127 D151
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

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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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