Structure of PDB 5yu9 Chain C

Receptor sequence
>5yu9C (length=306) Species: 9606 (Homo sapiens) [Search protein sequence]
EAPNQALLRILKETEFKKIKVLGSGAFGTVYKGLWIPEGEKVKIPVAIKE
LREKANKEILDEAYVMASVDNPHVCRLLGICLTSTVQLIMQLMPFGCLLD
YVREHKDNIGSQYLLNWCVQIAKGMNYLEDRRLVHRDLAARNVLVKTPQH
VKITDFGLAKLLKVPIKWMALESILHRIYTHQSDVWSYGVTVWELMTFGS
KPYDGIPASEISSILEKGERLPQPPICTIDVYMIMVKCWMIDADSRPKFR
ELIIEFSKMARDPQRYLVIQGDERMHLPSPTDSNFYRALMDEEDMVDADE
YLIPQQ
3D structure
PDB5yu9 Ibrutinib targets mutant-EGFR kinase with a distinct binding conformation.
ChainC
Resolution1.95 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) D837 A839 R841 N842 D855
Catalytic site (residue number reindexed from 1) D137 A139 R141 N142 D155
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 1E8 C V726 A743 M790 M793 G796 C797 D800 T854 D855 F856 V30 A47 M90 M93 G96 C97 D100 T154 D155 F156 BindingDB: IC50=0.5nM,Kd=6.9nM
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:5yu9, PDBe:5yu9, PDBj:5yu9
PDBsum5yu9
PubMed27626175
UniProtP00533|EGFR_HUMAN Epidermal growth factor receptor (Gene Name=EGFR)

[Back to BioLiP]