Structure of PDB 6urc Chain B

Receptor sequence
>6urcB (length=398) Species: 9606 (Homo sapiens) [Search protein sequence]
ETSVVIVGKISFCPKDVLGHGAEGTIVYRGMFDNRDVAVKRILPECFSFA
DREVQLLRESDEHPNVIRYFCTEKDRQFQYIAIELCAATLQEYVEQKDFA
HLGLEPITLLQQTTSGLAHLHSLNIVHRDLKPHNILISMPNAHGKIKAMI
SDFGLCKKLAVGRHSFSRRSGVPGTEGWIAPEMLSEDCKENPTYTVDIFS
AGCVFYYVISEGSHPFGKSLQRQANILLGACSLDCLHPEKHEDVIARELI
EKMIAMDPQKRPSAKHVLKHPFFWSLEKQLQFFQDVSDRIEKESLDGPIV
KQLERGGRAVVKMDWRENITVPLQTDYKGGSVRDLLRAMRNKKHHYRELP
AEVRETLGSLPDDFVCYFTSRFPHLLAHTYRAMELCSHERLFQPYYFH
3D structure
PDB6urc Disruption of IRE1 alpha through its kinase domain attenuates multiple myeloma.
ChainB
Resolution2.2 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) D129 K131 N134 D152 T175
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 QFV B L577 A597 K599 E612 Y628 I640 I642 L644 C645 E651 S710 D711 L18 A38 K40 E53 Y69 I81 I83 L85 C86 E92 S151 D152 BindingDB: IC50=13nM
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:6urc, PDBe:6urc, PDBj:6urc
PDBsum6urc
PubMed31371506
UniProtO75460|ERN1_HUMAN Serine/threonine-protein kinase/endoribonuclease IRE1 (Gene Name=ERN1)

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