Structure of PDB 4lqm Chain A

Receptor sequence
>4lqmA (length=305) Species: 9606 (Homo sapiens) [Search protein sequence]
EAPNQALLRILKETEFKKIKVLGSGAFGTVYKGLWIPEGEKVKIPVAIKE
LTSPKANKEILDEAYVMASVDNPHVCRLLGICLTSTVQLITQLMPFGCLL
DYVREHKDNIGSQYLLNWCVQIAKGMNYLEDRRLVHRDLAARNVLVKTPQ
HVKITDFGRAKLLGAEEGKVPIKWMALESILHRIYTHQSDVWSYGVTVWE
LMTFGSKPYDGIPASEISSILEKGERLPQPPICTIDVYMIMVKCWMIDAD
SRPKFRELIIEFSKMARDPQRYLVIQGDERMHLPSALMDEEDMDDVVDAD
EYLIP
3D structure
PDB4lqm Structural, Biochemical, and Clinical Characterization of Epidermal Growth Factor Receptor (EGFR) Exon 20 Insertion Mutations in Lung Cancer.
ChainA
Resolution2.5 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
Catalytic site (residue number reindexed from 1) D138 A140 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 DJK A A743 K745 E762 L788 T790 M793 C797 D800 L844 A47 K49 E63 L89 T91 M94 C98 D101 L145 BindingDB: IC50=2nM
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:4lqm, PDBe:4lqm, PDBj:4lqm
PDBsum4lqm
PubMed24353160
UniProtP00533|EGFR_HUMAN Epidermal growth factor receptor (Gene Name=EGFR)

[Back to BioLiP]