Structure of PDB 4yz9 Chain B

Receptor sequence
>4yz9B (length=375) Species: 9606 (Homo sapiens) [Search protein sequence]
VVIVGKISFCPKDVLGHGAEGTIVYRGMFDNRDVAVKRILPECFSFADRE
VQLLRESDEHPNVIRYFCTEKDRQFQYIAIELCAATLQEYVEQKDFAHLG
LEPITLLQQTTSGLAHLHSLNIVHRDLKPHNILISMPNAHGKIKAMISDF
GLCEGWIAPEMLSNPTYTVDIFSAGCVFYYVISEGSHPFGKSLQRQANIL
LGACSLDCLHPEKHEDVIARELIEKMIAMDPQKRPSAKHVLKHPFFWSLE
KQLQFFQDVSDRIEKESLDGPIVKQLERGGRAVVKMDWRENITVPLQTDL
FRTYKGGSVRDLLRAMRNKKHHYRELPAEVRETLGSLPDDFVCYFTSRFP
HLLAHTYRAMELCSHERLFQPYYFH
3D structure
PDB4yz9 Long-Range Inhibitor-Induced Conformational Regulation of Human IRE1 alpha Endoribonuclease Activity.
ChainB
Resolution2.463 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
Catalytic site (residue number reindexed from 1) D126 K128 N131 D149
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 4K7 B K599 A609 E612 H686 R687 D711 K37 A47 E50 H124 R125 D149 MOAD: Ki=200nM
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:4yz9, PDBe:4yz9, PDBj:4yz9
PDBsum4yz9
PubMed26438213
UniProtO75460|ERN1_HUMAN Serine/threonine-protein kinase/endoribonuclease IRE1 (Gene Name=ERN1)

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