Structure of PDB 4li5 Chain A

Receptor sequence
>4li5A (length=306) Species: 9606 (Homo sapiens) [Search protein sequence]
GSMGEAPNQALLRILKETEFKKIKVLGSGAFGTVYKGLWIPEGEKVKIPV
AIKELREATSPKANKEILDEAYVMASVDNPHVCRLLGICLTSTVQLITQL
MPFGCLLDYVREHKDNIGSQYLLNWCVQIAKGMNYLEDRRLVHRDLAARN
VLVKTPQHVKITDFGLAKLLGAEEKEYHAEGGKVPIKWMALESILHRIYT
HQSDVWSYGVTVWELMTFGSKPYDGIPASEISSILEKGERLPQPPICTID
VYMIMVKCWMIDADSRPKFRELIIEFSKMARDPQRYLVIQGDEDDVVDAD
EYLIPQ
3D structure
PDB4li5 Structure- and Reactivity-Based Development of Covalent Inhibitors of the Activating and Gatekeeper Mutant Forms of the Epidermal Growth Factor Receptor (EGFR).
ChainA
Resolution2.64 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 G874
Catalytic site (residue number reindexed from 1) D145 A147 R149 N150 D163 G182
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 1WY A L718 G719 F723 V726 A743 M793 G796 C797 D800 L844 L26 G27 F31 V34 A51 M101 G104 C105 D108 L152 PDBbind-CN: -logKd/Ki=6.26,IC50=0.55uM
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:4li5, PDBe:4li5, PDBj:4li5
PDBsum4li5
PubMed23930994
UniProtP00533|EGFR_HUMAN Epidermal growth factor receptor (Gene Name=EGFR)

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