Structure of PDB 4riy Chain B

Receptor sequence
>4riyB (length=293) Species: 9606 (Homo sapiens) [Search protein sequence]
LVEPLTPSGEAPNQALLRILKETEFKKIKVLGSGAFGTVYKGLWIPEGEK
VKIPVAIKELREATSPKANKEILDEAYVMASVDNPHVCRLLGICLTSTVQ
LITQLMPFGCLLDYVREHKDNIGSQYLLNWCVQIAKGMNYLEDRRLVHRD
LAARNVLVKTPQHVKITDFGLAKLLGAEEKEYHAVPIKWMALESILHRIY
THQSDVWSYGVTVWELMTFGSKPYDGIPASEISSILEKGERLPQPPICTI
DVYMIMRKCWMIDADSRPKFRELIIEFSKMARDPQRYLVIQGD
3D structure
PDB4riy Structural analysis of the EGFR/HER3 heterodimer reveals the molecular basis for activating HER3 mutations.
ChainB
Resolution2.981 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D813 A815 R817 N818 D831
Catalytic site (residue number reindexed from 1) D150 A152 R154 N155 D168
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 ADP B F699 A719 K721 L768 M769 L820 D831 F36 A56 K58 L105 M106 L157 D168
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

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Biological Process
External links
PDB RCSB:4riy, PDBe:4riy, PDBj:4riy
PDBsum4riy
PubMed25468994
UniProtP00533|EGFR_HUMAN Epidermal growth factor receptor (Gene Name=EGFR)

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