Structure of PDB 4pl5 Chain B

Receptor sequence

>4pl5B (length=383) Species: 10090 (Mus musculus)

RMVIVGKISFCPKDVLGHGAEGTIVYKGMFDNRDVAVKRILPECFSFADR
EVQLLRESDEHPNVIRYFCTEKDRQFQYIAIELCAATLQEYVEQKDFAHL
GLEPITLLHQTTSGLAHLHSLNIVHRDLKPHNILLSMPNAHGRIKAMISD
FGLCKKVPGTEGWIAPEMLSPTYTVDIFSAGCVFYYVISEGYHPFGKSLQ
RQANILLGACNLDCFHSDKHEDVIARELIEKMIAMDPQQRPSAKHVLKHP
FFWSLEKQLQFFQDVSDRIEKEALDGPIVRQLERGGRAVVKMDWRENITV
PLQTDLRKFRTYKGGSVRDLLRAMRNKKHHYRELPVEVQETLGSIPDDFV
RYFTSRFPHLLSHTYQAMELCRHERLFQTYYWH

3D structure

• PDB: 4pl5 Structure and mechanism of action of the hydroxy-aryl-aldehyde class of IRE1 endoribonuclease inhibitors.
• Chain: B
• Resolution: 3.4 Å

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	ADP	B	G580 V586 K599 C645 H692 D711	G19 V25 K38 C84 H131 D150
BS02	MG	B	H692 D711	H131 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

External links

• PDB: RCSB:4pl5, PDBe:4pl5, PDBj:4pl5
• PDBsum: 4pl5
• PubMed: 25164867
• UniProt: Q9EQY0|ERN1_MOUSE Serine/threonine-protein kinase/endoribonuclease IRE1 (Gene Name=Ern1)