Structure of PDB 6p8q Chain D

Receptor sequence
>6p8qD (length=296) Species: 9606 (Homo sapiens) [Search protein sequence]
NQALLRILKETEFKKIKVLGSGAFGTVYKGLWIPEGEKVKIPVAIKELRE
ATSPKANKEILDEAYVMASVDNPHVCRLLGICLTSTVQLIMQLMPFGCLL
DYVREHKDNIGSQYLLNWCVQIAKGMNYLEDRRLVHRDLAARNVLVKTPQ
HVKITDFGLAKLLGVPIKWMALESILHRIYTHQSDVWSYGVTVWELMTFG
SKPYDGIPASEISSILEKGERLPQPPICTIDVYMIMRKCWMIDADSRPKF
RELIIEFSKMARDPQRYLVIQGDERMHLPSPTDSNFYRALMDEEDM
3D structure
PDB6p8q Discovery and Optimization of Dibenzodiazepinones as Allosteric Mutant-Selective EGFR Inhibitors.
ChainD
Resolution1.9 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 R841 N842 D855
Catalytic site (residue number reindexed from 1) D138 R142 N143 D156
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 AMP D L718 G721 V726 A743 K745 M790 M793 R841 L844 D855 L19 G22 V27 A44 K46 M91 M94 R142 L145 D156
BS02 O57 D K745 M766 C775 L788 M790 D855 F856 L858 K46 M67 C76 L89 M91 D156 F157 L159
BS03 MG D G721 F723 K745 G22 F24 K46
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:6p8q, PDBe:6p8q, PDBj:6p8q
PDBsum6p8q
PubMed31749909
UniProtP00533|EGFR_HUMAN Epidermal growth factor receptor (Gene Name=EGFR)

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