Structure of PDB 6duk Chain D

Receptor sequence
>6dukD (length=307) Species: 9606 (Homo sapiens) [Search protein sequence]
QALLRILKETEFKKIKVLGSGAFGTVYKGLWIPEGEKVKIPVAIKELREA
TSPKANKEILDEAYVMASVDNPHVCRLLGICLTSTVQLIMQLMPFGCLLD
YVREHKDNIGSQYLLNWCVQIAKGMNYLEDRRLVHRDLAARNVLVKTPQH
VKITDFGLAKLLGAEEKEYHAEGGKVPIKWMALESILHRIYTHQSDVWSY
GVTVWELMTFGSKPYDGIPASEISSILEKGERLPQPPICTIDVYMIMRKC
WMIDADSRPKFRELIIEFSKMARDPQRYLVIQGDERMHLPSPTDSNFYRA
LMDEEDM
3D structure
PDB6duk Single and Dual Targeting of Mutant EGFR with an Allosteric Inhibitor.
ChainD
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) 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 MG D N842 D855 N142 D155
BS02 ANP D G719 S720 G721 V726 A743 K745 M790 L792 M793 D837 R841 N842 G19 S20 G21 V26 A43 K45 M90 L92 M93 D137 R141 N142
BS03 JBJ D F723 V726 A743 K745 I759 M766 R776 L777 L788 M790 D855 F856 L858 L861 E865 F23 V26 A43 K45 I59 M66 R76 L77 L88 M90 D155 F156 L158 L161 E165 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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