Structure of PDB 5hcy Chain A

Receptor sequence
>5hcyA (length=302) Species: 9606 (Homo sapiens) [Search protein sequence]
GEAPNQALLRILKETEFKKIKVLGSGAFGTVYKGLWIPEGEKVKIPVAIK
ELATSPKANKEILDEAYVMASVDNPHVCRLLGICLTSTVQLIMQLMPFGC
LLDYVREHKDNIGSQYLLNWCVQIAKGMNYLEDRRLVHRDLAARNVLVKT
PQHVKITDFGRAKLLVPIKWMALESILHRIYTHQSDVWSYGVTVWELMTF
GSKPYDGIPASEISSILEKGERLPQPPICTIDVYMIMVKCWMIDADSRPK
FRELIIEFSKMARDPQRYLVIQGDERMHLPSPTDSNFYDMDDVVDADEYL
IP
3D structure
PDB5hcy Discovery of a Noncovalent, Mutant-Selective Epidermal Growth Factor Receptor Inhibitor.
ChainA
Resolution2.46 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) D140 A142 R144 N145 D158
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 60D A L718 F723 A743 K745 M766 C775 M790 Q791 M793 G796 N842 L844 T854 D855 L23 F28 A48 K50 M69 C78 M93 Q94 M96 G99 N145 L147 T157 D158 MOAD: Ki=1.2nM
PDBbind-CN: -logKd/Ki=8.92,Ki=1.2nM
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:5hcy, PDBe:5hcy, PDBj:5hcy
PDBsum5hcy
PubMed27564586
UniProtP00533|EGFR_HUMAN Epidermal growth factor receptor (Gene Name=EGFR)

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