Structure of PDB 4riw Chain D

Receptor sequence
>4riwD (length=297) Species: 9606 (Homo sapiens) [Search protein sequence]
LVEPLTPSGEAPNQALLRILKETEFKKIKVLGSGAFGTVYKGLWIPEGEK
VKIPVAIKELREATSPKANKEILDEAYVMASVDNPHVCRLLGICLTSTVQ
LITQLMPFGCLLDYVREHKDNIGSQYLLNWCVQIAKGMNYLEDRRLVHRD
LAARNVLVKTPQHVKITDFGLAKLLGAEEKEYHAEGGKVPIKWMALESIL
HRIYTHQSDVWSYGVTVWELMTFGSKPYDGIPASEISSILEKGERLPQPP
ICTIDVYMIMRKCWMIDADSRPKFRELIIEFSKMARDPQRYLVIQGD
3D structure
PDB4riw Structural analysis of the EGFR/HER3 heterodimer reveals the molecular basis for activating HER3 mutations.
ChainD
Resolution3.1 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 G850
Catalytic site (residue number reindexed from 1) D150 A152 R154 N155 D168 G187
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 D F699 V702 A719 K721 Q767 M769 L820 D831 F36 V39 A56 K58 Q104 M106 L157 D168
BS02 MG D N818 D831 N155 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

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Molecular Function
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Biological Process
External links
PDB RCSB:4riw, PDBe:4riw, PDBj:4riw
PDBsum4riw
PubMed25468994
UniProtP00533|EGFR_HUMAN Epidermal growth factor receptor (Gene Name=EGFR)

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