Structure of PDB 6hv0 Chain A

Receptor sequence
>6hv0A (length=377) Species: 9606 (Homo sapiens) [Search protein sequence]
SVVIVGKISFCPKDVLGHGAEGTIVYRGMFDNRDVAVKRILPECSDEHPN
VIRYFCTEKDRQFQYIAIELCAATLQEYVEQKDFGLEPITLLQQTTSGLA
HLHSLNIVHRDLKPHNILISMPNAHGKIKAMISDFGLCKKLAVGRHSFSR
RSGVPGTEGWIAPEMNPTYTVDIFSAGCVFYYVISEGSHPFGKSLQRQAN
ILLGACSLDCLHPEKHEDVIARELIEKMIAMDPQKRPSAKHVLKHPFFWS
LEKQLQFFQDVSDRIEKESLDGPIVKQLERGGRAVVKMDWRENITVPLQT
DLRRTYKGGSVRDLLRAMRNKKHHYRELPAEVRETLGSLPDDFVCYFTSR
FPHLLAHTYRAMELCSHERLFQPYYFH
3D structure
PDB6hv0 Binding to an Unusual Inactive Kinase Conformation by Highly Selective Inhibitors of Inositol-Requiring Enzyme 1 alpha Kinase-Endoribonuclease.
ChainA
Resolution2.73 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) D111 K113 N116 D134 T157
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 GUK A L577 K599 I642 L644 C645 F712 L714 L16 K38 I68 L70 C71 F135 L137 PDBbind-CN: -logKd/Ki=6.56,IC50=276nM
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
View graph for
Biological Process
External links
PDB RCSB:6hv0, PDBe:6hv0, PDBj:6hv0
PDBsum6hv0
PubMed30779566
UniProtO75460|ERN1_HUMAN Serine/threonine-protein kinase/endoribonuclease IRE1 (Gene Name=ERN1)

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