Structure of PDB 6w3k Chain A

Receptor sequence
>6w3kA (length=398) Species: 9606 (Homo sapiens) [Search protein sequence]
SVVIVGKISFCPKDVLGHGAEGTIVYRGMFDNRDVAVKRILPECFSFADR
EVQLLRESDEHPNVIRYFCTEKDRQFQYIAIELCAATLQEYVEQKDFAHL
GLEPITLLQQTTSGLAHLHSLNIVHRDLKPHNILISMPNAHGKIKAMISD
FGLCKKLAVGRHSFSRPGTEGWIAPEMLSEDCKENPTYTVDIFSAGCVFY
YVISEGSHPFGKSLQRQANILLGACSLDCLHPEKHEDVIARELIEKMIAM
DPQKRPSAKHVLKHPFFWSLEKQLQFFQDVSDRIEKESLDGPIVKQLERG
GRAVVKMDWRENITVPLQTDLRKFRTYKGGSVRDLLRAMRNKKHHYRELP
AEVRETLGSLPDDFVCYFTSRFPHLLAHTYRAMELCSHERLFQPYYFH
3D structure
PDB6w3k Activation of the IRE1 RNase through remodeling of the kinase front pocket by ATP-competitive ligands.
ChainA
Resolution2.08 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 T169
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 SJS A L577 V586 A597 K599 I626 I642 C645 A646 A647 E651 H692 L695 D711 L16 V25 A36 K38 I65 I81 C84 A85 A86 E90 H131 L134 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:6w3k, PDBe:6w3k, PDBj:6w3k
PDBsum6w3k
PubMed33318494
UniProtO75460|ERN1_HUMAN Serine/threonine-protein kinase/endoribonuclease IRE1 (Gene Name=ERN1)

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