Structure of PDB 5gty Chain A

Receptor sequence
>5gtyA (length=300) Species: 9606 (Homo sapiens) [Search protein sequence]
NQALLRILKETEFKKIKVLGSGAFGTVYKGLWIPEGEKVKIPVAIKELRE
KANKEILDEAYVMASVDNPHVCRLLGICLTSTVQLIMQLMPFGCLLDYVR
EHKDNIGSQYLLNWCVQIAKGMNYLEDRRLVHRDLAARNVLVKTPQHVKI
TDFGLAKLLGKVPIKWMALESILHRIYTHQSDVWSYGVTVWELMTFGSKP
YDGIPASEISSILEKGERLPQPPICTIDVYMIMVKCWMIDADSRPKFREL
IIEFSKMARDPQRYLVIQGDERMHLPSPTDSNFYRALMDEEDMDDVVDAD
3D structure
PDB5gty Discovery and characterization of a novel irreversible EGFR mutants selective and potent kinase inhibitor CHMFL-EGFR-26 with a distinct binding mode.
ChainA
Resolution3.14 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) D134 A136 R138 N139 D152
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 816 A G719 V726 A743 I744 K745 R776 L777 M790 M793 G796 C797 R841 L844 D855 G20 V27 A44 I45 K46 R73 L74 M87 M90 G93 C94 R138 L141 D152 PDBbind-CN: -logKd/Ki=7.72,IC50=19.01nM
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:5gty, PDBe:5gty, PDBj:5gty
PDBsum5gty
PubMed28407693
UniProtP00533|EGFR_HUMAN Epidermal growth factor receptor (Gene Name=EGFR)

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