Structure of PDB 6w39 Chain B

Receptor sequence
>6w39B (length=374) Species: 9606 (Homo sapiens) [Search protein sequence]
VVIVGKISFCPKDVLGHGAEGTIVYRGMFDNRDVAVKRILPECFSFADRE
VQLLRESDEHPNVIRYFCTEKDRQFQYIAIELCAATLQEYVEQFAHLGLE
PITLLQQTTSGLAHLHSLNIVHRDLKPHNILISMPNAHGKIKAMISDFGL
TEGWIAPEMLSENPTYTVDIFSAGCVFYYVISEGSHPFGKSLQRQANILL
GACSLDCLHPEKHEDVIARELIEKMIAMDPQKRPSAKHVLKHPFFWSLEK
QLQFFQDVSDRIEKESLDGPIVKQLERGGRAVVKMDWRENITVPLQTDLR
RTYKGGSVRDLLRAMRNKKHHYRELPAEVRETLGSLPDDFVCYFTSRFPH
LLAHTYRAMELCSHERLFQPYYFH
3D structure
PDB6w39 Activation of the IRE1 RNase through remodeling of the kinase front pocket by ATP-competitive ligands.
ChainB
Resolution1.736 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) D124 K126 N129 D147 T151
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 SJG B A597 K599 E612 I642 C645 E651 S710 D711 F712 A35 K37 E50 I80 C83 E89 S146 D147 F148
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:6w39, PDBe:6w39, PDBj:6w39
PDBsum6w39
PubMed33318494
UniProtO75460|ERN1_HUMAN Serine/threonine-protein kinase/endoribonuclease IRE1 (Gene Name=ERN1)

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