Structure of PDB 3p23 Chain D

Receptor sequence
>3p23D (length=387) Species: 9606 (Homo sapiens) [Search protein sequence]
TSVVIVGKISFCPKDVLGHGAEGTIVYRGMFDNRDVAVKRILPECFSFAD
REVQLLRESDEHPNVIRYFCTEKDRQFQYIAIELCAATLQEYVEQKDFAH
LGLEPITLLQQTTSGLAHLHSLNIVHRDLKPHNILISMPNAHGKIKAMIS
DFGLCKKPGTEGWIAPEMLSEDCNPTYTVDIFSAGCVFYYVISEGSHPFG
KSLQRQANILLGACSLDCLHPEKHEDVIARELIEKMIAMDPQKRPSAKHV
LKHPFFWSLEKQLQFFQDVSDRIEKESLDGPIVKQLERGGRAVVKMDWRE
NITVPLQTDLRKFRTYKGGSVRDLLRAMRNKKHHYRELPAEVRETLGTLP
DDFVCYFTSRFPHLLAHTYRAMELCSHERLFQPYYFH
3D structure
PDB3p23 Structure of the Ire1 autophosphorylation complex and implications for the unfolded protein response.
ChainD
Resolution2.7 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) D128 K130 N133 D151 T160
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 ADP D L577 G578 G580 K599 I642 C645 K690 L695 D711 L17 G18 G20 K39 I82 C85 K130 L135 D151
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:3p23, PDBe:3p23, PDBj:3p23
PDBsum3p23
PubMed21317875
UniProtO75460|ERN1_HUMAN Serine/threonine-protein kinase/endoribonuclease IRE1 (Gene Name=ERN1)

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