Structure of PDB 7ju6 Chain A

Receptor sequence
>7ju6A (length=288) Species: 9606 (Homo sapiens) [Search protein sequence]
EDPKWEFPRKNLVLGKTLGEGEFGKVVKATAFHLKGRAGYTTVAVKMLKE
NASPSELRDLLSEFNVLKQVNHPHVIKLYGACSQDGPLLLIVEYAKYGSL
RGFLRESRKVGPGYLGPDERALTMGDLISFAWQISQGMQYLAEMKLVHRD
LAARNILVAEGRKMKISDFGLSRDVYEEDSYVKRSQGRIPVKWMAIESLF
DHIYTTQSDVWSFGVLLWEIVTLGGNPYPGIPPERLFNLLKTGHRMERPD
NCSEEMYRLMLQCWKQEPDKRPVFADISKDLEKMMVKR
3D structure
PDB7ju6 Structural basis of acquired resistance to selpercatinib and pralsetinib mediated by non-gatekeeper RET mutations.
ChainA
Resolution2.06 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Catalytic site (original residue number in PDB) D874 A876 R878 N879 D892
Catalytic site (residue number reindexed from 1) D150 A152 R154 N155 D168
Enzyme Commision number 2.7.10.1: receptor protein-tyrosine kinase.
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 Q6G A L730 G731 G736 K737 V738 A756 A807 G810 L881 L18 G19 G24 K25 V26 A44 A95 G98 L157 BindingDB: IC50=14.0nM
Gene Ontology
Molecular Function
GO:0004672 protein kinase activity
GO:0004713 protein tyrosine kinase activity
GO:0005524 ATP binding
Biological Process
GO:0006468 protein phosphorylation

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:7ju6, PDBe:7ju6, PDBj:7ju6
PDBsum7ju6
PubMed33161056
UniProtP07949|RET_HUMAN Proto-oncogene tyrosine-protein kinase receptor Ret (Gene Name=RET)

[Back to BioLiP]