Structure of PDB 6duk Chain E

Receptor sequence
>6dukE (length=298) Species: 9606 (Homo sapiens) [Search protein sequence]
APNQALLRILKETEFKKIKVLGSGAFGTVYKGLWIPEGEKVKIPVAIKEL
REATSPKANKEILDEAYVMASVDNPHVCRLLGICLTSTVQLIMQLMPFGC
LLDYVREHKDNIGSQYLLNWCVQIAKGMNYLEDRRLVHRDLAARNVLVKT
PQHVKITDFGLAKLLKVPIKWMALESILHRIYTHQSDVWSYGVTVWELMT
FGSKPYDGIPASEISSILEKGERLPQPPICTIDVYMIMRKCWMIDADSRP
KFRELIIEFSKMARDPQRYLVIQGDERMHLPSPTDSNFYRALMDEEDM
3D structure
PDB6duk Single and Dual Targeting of Mutant EGFR with an Allosteric Inhibitor.
ChainE
Resolution2.2 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D837 A839 R841 N842 D855
Catalytic site (residue number reindexed from 1) D140 A142 R144 N145 D158
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 MG E N842 D855 N145 D158
BS02 ANP E S720 G721 A722 V726 A743 K745 M790 L792 M793 D837 R841 N842 L844 S23 G24 A25 V29 A46 K48 M93 L95 M96 D140 R144 N145 L147
BS03 JBJ E A743 K745 L747 M766 R776 L777 L788 M790 D855 F856 L858 L861 L862 A46 K48 L50 M69 R79 L80 L91 M93 D158 F159 L161 L164 L165 BindingDB: IC50=>1000nM
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

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Molecular Function
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Biological Process
External links
PDB RCSB:6duk, PDBe:6duk, PDBj:6duk
PDBsum6duk
PubMed31092401
UniProtP00533|EGFR_HUMAN Epidermal growth factor receptor (Gene Name=EGFR)

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