Structure of PDB 4ll0 Chain A

Receptor sequence
>4ll0A (length=291) Species: 9606 (Homo sapiens) [Search protein sequence]
EAPNQALLRILKETEFKKIKVLGSGAFGTVYKGLWIPEGEKVKIPVAIKE
LREATSPKANKEILDEAYVMASVDNPHVCRLLGICLTSTVQLIMQLMPFG
CLLDYVREHKDNIGSQYLLNWCVQIAKGMNYLEDRRLVHRDLAARNVLVK
TPQHVKITDFGRAKLLVPIKWMALESILHRIYTHQSDVWSYGVTVWELMT
FGSKPYDGIPASEISSILEKGERLPQPPICTIDVYMIMVKCWMIDADSRP
KFRELIIEFSKMARDPQRYLVIQGDERMEEDMDVVDADEYL
3D structure
PDB4ll0 Mechanism for activation of mutated epidermal growth factor receptors in lung cancer.
ChainA
Resolution4.0 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) D141 A143 R145 N146 D159
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 YUN A L718 V726 A743 M790 Q791 L792 M793 C797 D800 L844 L22 V30 A47 M94 Q95 L96 M97 C101 D104 L148 BindingDB: IC50=2.62nM
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:4ll0, PDBe:4ll0, PDBj:4ll0
PDBsum4ll0
PubMed24019492
UniProtP00533|EGFR_HUMAN Epidermal growth factor receptor (Gene Name=EGFR)

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