Structure of PDB 3sdj Chain B

Receptor sequence
>3sdjB (length=418) Species: 559292 (Saccharomyces cerevisiae S288C) [Search protein sequence]
LKNLVVSEKILGYGSSGTVVFQGSFQGRPVAVKRMLIDFCDIALMEIKLL
TESDDHPNVIRYYCSETTDRFLYIALELCNLNLQDLVESKNVSDENLKLQ
KEYNPISLLRQIASGVAHLHSLKIIHRDLKPQNILVSTSSRFTADQQTGA
ENLRILISDFGLCKKLDSGQSSFRTNLNNPSGTSGWRAPELLEESTKRRL
TRSIDIFSMGCVFYYILSKGKHPFGDKYSRESNIIRGIFSLDEMKCLHDR
SLIAEATDLISQMIDHDPLKRPTAMKVLRHPLFWPKSKKLEFLLKVSDRL
EIENRDPPSALLMKFDAGSDFVIPSGDWTVKFDKTFMDNLERYRKYHSSK
LMDLLRALRNKYHNFMDLPEDIAELMGPVPDGFYDYFTKRFPNLLIGVYM
IVKENLSDDQILREFLYS
3D structure
PDB3sdj Structural and functional basis for RNA cleavage by Ire1.
ChainB
Resolution3.65 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D797 K799 N802 D828 T852
Catalytic site (residue number reindexed from 1) D128 K130 N133 D159 T183
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 APJ B L680 Y682 A700 C748 L804 L11 Y13 A31 C79 L135
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
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Biological Process
External links
PDB RCSB:3sdj, PDBe:3sdj, PDBj:3sdj
PDBsum3sdj
PubMed21729333
UniProtP32361|IRE1_YEAST Serine/threonine-protein kinase/endoribonuclease IRE1 (Gene Name=IRE1)

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