Structure of PDB 7ju5 Chain A

Receptor sequence
>7ju5A (length=287) Species: 9606 (Homo sapiens) [Search protein sequence]
GPLSLSVDAFKILEDPKWEFPRKNLVLGKTLGEGEFGKVVKATAFHLKGR
AGYTTVAVKMLKENASPSELRDLLSEFNVLKQVNHPHVIKLYGACSQDGP
LLLIVEYAKYGSLRGFLRESRKVGERALTMGDLISFAWQISQGMQYLAEM
KLVHRDLAARNILVAEGRKMKISDFGLSRDVYSQGRIPVKWMAIESLFDH
IYTTQSDVWSFGVLLWEIVTLGGNPYPGIPPERLFNLLKTGHRMERPDNC
SEEMYRLMLQCWKQEPDKRPVFADISKDLEKMMVKRR
3D structure
PDB7ju5 Structural basis of acquired resistance to selpercatinib and pralsetinib mediated by non-gatekeeper RET mutations.
ChainA
Resolution1.9 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) D156 A158 R160 N161 D174
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 Q4J A L730 G731 E732 G733 G736 K737 V738 A756 M759 E805 Y806 A807 G810 L881 L31 G32 E33 G34 G37 K38 V39 A57 M60 E106 Y107 A108 G111 L163 BindingDB: IC50=6000nM
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:7ju5, PDBe:7ju5, PDBj:7ju5
PDBsum7ju5
PubMed33161056
UniProtP07949|RET_HUMAN Proto-oncogene tyrosine-protein kinase receptor Ret (Gene Name=RET)

[Back to BioLiP]