Structure of PDB 4rix Chain B

Receptor sequence
>4rixB (length=293) Species: 9606 (Homo sapiens) [Search protein sequence]
LVEPLTPSGEAPNQALLRILKETEFKKIKVLGSGAFGTVYKGLWIPEGEK
VKIPVAIKELREATSPKANKEILDEAYVMASVDNPHVCRLLGICLTSTVQ
LITQLMPFGCLLDYVREHKDNIGSQYLLNWCVQIAKGMNYLEDRRLVHRD
LAARNVLVKTPQHVKITDFGLAKLLGAEEKEYHAVPIKWMALESILHRIY
THQSDVWSYGVTVWELMTFGSKPYDGIPASEISSILEKGERLPQPPICTI
DVYMIMRKCWMIDADSRPKFRELIIEFSKMARDPQRYLVIQGD
3D structure
PDB4rix Structural analysis of the EGFR/HER3 heterodimer reveals the molecular basis for activating HER3 mutations.
ChainB
Resolution3.1 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
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 L694 F699 A719 L768 M769 G772 C773 L820 D831 L31 F36 A56 L105 M106 G109 C110 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
View graph for
Biological Process
External links
PDB RCSB:4rix, PDBe:4rix, PDBj:4rix
PDBsum4rix
PubMed25468994
UniProtP00533|EGFR_HUMAN Epidermal growth factor receptor (Gene Name=EGFR)

[Back to BioLiP]