Structure of PDB 7a2a Chain A

Receptor sequence
>7a2aA (length=266) Species: 9606 (Homo sapiens) [Search protein sequence]
NQALLRILKETEFKKIKVLGSGAFGTVYKGLWIPEGEKVKIPVAIKELRE
ATSANKEILDEAYVMASVDNPHVCRLLGICLTSTVQLIMQLMPFGCLLDY
VREHKDNIGSQYLLNWCVQIAKGMNYLEDRRLVHRDLAARNVLVKTPQHV
KITDFGLVPIKWMALESILHRIYTHQSDVWSYGVTVWELMTFGSKPYDGI
PASEISSILEKGERLPQPPICTIDVYMIMRKCWMIDADSRPKFRELIIEF
SKMARDPQRYLVIQGD
3D structure
PDB7a2a Complex Crystal Structures of EGFR with Third-Generation Kinase Inhibitors and Simultaneously Bound Allosteric Ligands.
ChainA
Resolution1.9 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) D837 R841 N842 D855
Catalytic site (residue number reindexed from 1) D136 R140 N141 D154
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 57N A A743 K745 M766 L788 M790 D855 F856 A44 K46 M65 L87 M89 D154 F155 BindingDB: IC50=>50000nM
BS02 7G9 A V726 A743 L792 M793 G796 C797 R841 V27 A44 L91 M92 G95 C96 R140
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:7a2a, PDBe:7a2a, PDBj:7a2a
PDBsum7a2a
PubMed33335671
UniProtP00533|EGFR_HUMAN Epidermal growth factor receptor (Gene Name=EGFR)

[Back to BioLiP]