Structure of PDB 4pl5 Chain C

Receptor sequence
>4pl5C (length=386) Species: 10090 (Mus musculus) [Search protein sequence]
RMVIVGKISFCPKDVLGHGAEGTIVYKGMFDNRDVAVKRILPECFSFADR
EVQLLRESDEHPNVIRYFCTEKDRQFQYIAIELCAATLQEYVEQKDFAHL
GLEPITLLHQTTSGLAHLHSLNIVHRDLKPHNILLSMPNAHGRIKAMISD
FGLCKKLAVPGTEGWIAPEMLSNPTYTVDIFSAGCVFYYVISEGYHPFGK
SLQRQANILLGACNLDCFHSDKHEDVIARELIEKMIAMDPQQRPSAKHVL
KHPFFWSLEKQLQFFQDVSDRIEKEALDGPIVRQLERGGRAVVKMDWREN
ITVPLQTDLRKFRTYKGGSVRDLLRAMRNKKHHYRELPVEVQETLGSIPD
DFVRYFTSRFPHLLSHTYQAMELCRHERLFQTYYWH
3D structure
PDB4pl5 Structure and mechanism of action of the hydroxy-aryl-aldehyde class of IRE1 endoribonuclease inhibitors.
ChainC
Resolution3.4 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D688 K690 N693 D711 T734
Catalytic site (residue number reindexed from 1) D127 K129 N132 D150 T162
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 ADP C H579 G580 V586 A597 K690 H692 N693 L695 H18 G19 V25 A36 K129 H131 N132 L134
BS02 MG C N693 D711 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:4pl5, PDBe:4pl5, PDBj:4pl5
PDBsum4pl5
PubMed25164867
UniProtQ9EQY0|ERN1_MOUSE Serine/threonine-protein kinase/endoribonuclease IRE1 (Gene Name=Ern1)

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