Structure of PDB 5j9y Chain A

Receptor sequence
>5j9yA (length=300) Species: 9606 (Homo sapiens) [Search protein sequence]
EAPNQALLRILKETEFKKIKVLGSGAFGTVYKGLWIPEGEKVKIPVAIKE
LREATSPKANKEILDEAYVMASVDNPHVCRLLGICLTSTVQLIMQLMPFG
CLLDYVREHKDNIGSQYLLNWCVQIAKGMNYLEDRRLVHRDLAARNVLVK
TPQHVKITDFGLAKLLEKEYHAEGGKVPIKWMALESILHRIYTHQSDVWS
YGVTVWELMTFGSKPYDGIPASEISSILEKGERLPQPPICTIDVYMIMVK
CWMIDADSRPKFRELIIEFSKMARDPQRYLVIQGDEDMDDVVDADEYLIP
3D structure
PDB5j9y Insight into the Inhibition of Drug-Resistant Mutants of the Receptor Tyrosine Kinase EGFR.
ChainA
Resolution2.8 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 G874
Catalytic site (residue number reindexed from 1) D141 A143 R145 N146 D159 G175
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 6HL A A743 K745 M790 M793 C797 D800 A47 K49 M94 M97 C101 D104 PDBbind-CN: -logKd/Ki=7.24,Ki=58nM
BindingDB: IC50=60nM
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:5j9y, PDBe:5j9y, PDBj:5j9y
PDBsum5j9y
PubMed27496389
UniProtP00533|EGFR_HUMAN Epidermal growth factor receptor (Gene Name=EGFR)

[Back to BioLiP]