Structure of PDB 4pl3 Chain B

Receptor sequence
>4pl3B (length=383) Species: 10090 (Mus musculus) [Search protein sequence]
RMVIVGKISFCPKDVLGHGAEGTIVYKGMFDNRDVAVKRILPECFSFADR
EVQLLRESDEHPNVIRYFCTEKDRQFQYIAIELCAATLQEYVEQKDFAHL
GLEPITLLHQTTSGLAHLHSLNIVHRDLKPHNILLSMPNAHGRIKAMISD
FGLCKKVPGTEGWIAPEMLSPTYTVDIFSAGCVFYYVISEGYHPFGKSLQ
RQANILLGACNLDCFHSDKHEDVIARELIEKMIAMDPQQRPSAKHVLKHP
FFWSLEKQLQFFQDVSDRIEKEALDGPIVRQLERGGRAVVKMDWRENITV
PLQTDLRKFRTYKGGSVRDLLRAMRNKKHHYRELPVEVQETLGSIPDDFV
RYFTSRFPHLLSHTYQAMELCRHERLFQTYYWH
3D structure
PDB4pl3 Structure and mechanism of action of the hydroxy-aryl-aldehyde class of IRE1 endoribonuclease inhibitors.
ChainB
Resolution2.9 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D688 K690 N693 D711 T734
Catalytic site (residue number reindexed from 1) D127 K129 N132 D150 T160
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 31J B L886 F889 Y892 N906 K907 H910 E913 L306 F309 Y312 N326 K327 H330 E333
BS02 ADP B L577 H579 G580 K599 C645 H692 D711 L16 H18 G19 K38 C84 H131 D150
BS03 MG B H692 N693 D711 H131 N132 D150
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:4pl3, PDBe:4pl3, PDBj:4pl3
PDBsum4pl3
PubMed25164867
UniProtQ9EQY0|ERN1_MOUSE Serine/threonine-protein kinase/endoribonuclease IRE1 (Gene Name=Ern1)

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