Structure of PDB 4yzd Chain C

Receptor sequence
>4yzdC (length=379) Species: 9606 (Homo sapiens) [Search protein sequence]
VVIVGKISFCPKDVLGHGAEGTIVYRGMFDNRDVAVKRILPECFSFADRE
VQLLRESDEHPNVIRYFCTEKDRQFQYIAIELCAATLQEYVEQHLGLEPI
TLLQQTTSGLAHLHSLNIVHRDLKPHNILISMPNAHGKIKAMISDFGLCK
KLVPGTEGWIAPEMLSNPTYTVDIFSAGCVFYYVISEGSHPFGKSLQRQA
NILLGACSLDCLHPEKHEDVIARELIEKMIAMDPQKRPSAKHVLKHPFFW
SLEKQLQFFQDVSDRIEKESLDGPIVKQLERGGRAVVKMDWRENITVPLQ
TDLRKFYKGGSVRDLLRAMRNKKHHYRELPAEVRETLGSLPDDFVCYFTS
RFPHLLAHTYRAMELCSHERLFQPYYFHE
3D structure
PDB4yzd Long-Range Inhibitor-Induced Conformational Regulation of Human IRE1 alpha Endoribonuclease Activity.
ChainC
Resolution3.102 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) D122 K124 N127 D145 T156
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 C L577 G578 H579 G580 A597 K599 I642 C645 T648 K690 H692 D711 L15 G16 H17 G18 A35 K37 I80 C83 T86 K124 H126 D145
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

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:4yzd, PDBe:4yzd, PDBj:4yzd
PDBsum4yzd
PubMed26438213
UniProtO75460|ERN1_HUMAN Serine/threonine-protein kinase/endoribonuclease IRE1 (Gene Name=ERN1)

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