Structure of PDB 4i24 Chain A

Receptor sequence
>4i24A (length=295) Species: 9606 (Homo sapiens) [Search protein sequence]
NQALLRILKETEFKKIKVLGSGAFGTVYKGLWIPEGEKVKIPVAIKELAN
KEILDEAYVMASVDNPHVCRLLGICLTSTVQLIMQLMPFGCLLDYVREHK
DNIGSQYLLNWCVQIAKGMNYLEDRRLVHRDLAARNVLVKTPQHVKITDF
GLAKLLVPIKWMALESILHRIYTHQSDVWSYGVTVWELMTFGSKPYDGIP
ASEISSILEKGERLPQPPICTIDVYMIMVKCWMIDADSRPKFRELIIEFS
KMARDPQRYLVIQGDERMHLPSPTDSNFYRALMDEEDMDDVVDAD
3D structure
PDB4i24 Insights into the Aberrant Activity of Mutant EGFR Kinase Domain and Drug Recognition.
ChainA
Resolution1.8 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 A839 R841 N842 D855
Catalytic site (residue number reindexed from 1) D131 A133 R135 N136 D149
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 1C9 A L718 A743 K745 L788 M790 L792 M793 G796 C797 D800 L844 D855 L19 A44 K46 L82 M84 L86 M87 G90 C91 D94 L138 D149 BindingDB: IC50=6.0nM
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:4i24, PDBe:4i24, PDBj:4i24
PDBsum4i24
PubMed23273428
UniProtP00533|EGFR_HUMAN Epidermal growth factor receptor (Gene Name=EGFR)

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