Structure of PDB 6p1l Chain D

Receptor sequence
>6p1lD (length=296) Species: 9606 (Homo sapiens) [Search protein sequence]
ALLRILKETEFKKIKVLGSGAFGTVYKGLWIPEGEKVKIPVAIKELREAT
SPKANKEILDEAYVMASVDNPHVCRLLGICLTSTVQLIMQLMPFGCLLDY
VREHKDNIGSQYLLNWCVQIAKGMNYLEDRRLVHRDLAARNVLVKTPQHV
KITDFGLVPIKWMALESILHRIYTHQSDVWSYGVTVWELMTFGSKPYDGI
PASEISSILEKGERLPQPPICTIDVYMIMRKCWMIDADSRPKFRELIIEF
SKMARDPQRYLVIQGDERMHLPSPTDSNFYRALMDEEDMDVVDADE
3D structure
PDB6p1l Discovery and Optimization of Dibenzodiazepinones as Allosteric Mutant-Selective EGFR Inhibitors.
ChainD
Resolution2.8 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) D136 R140 N141 D154
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 N141 D154
BS02 ANP D G719 G721 A722 V726 A743 K745 L792 M793 R841 N842 L844 D855 G18 G20 A21 V25 A42 K44 L91 M92 R140 N141 L143 D154
BS03 9LL D A743 K745 I759 M766 C775 R776 L777 L788 M790 D855 F856 L858 A42 K44 I58 M65 C74 R75 L76 L87 M89 D154 F155 L157 BindingDB: IC50=3.0nM
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:6p1l, PDBe:6p1l, PDBj:6p1l
PDBsum6p1l
PubMed31749909
UniProtP00533|EGFR_HUMAN Epidermal growth factor receptor (Gene Name=EGFR)

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