Structure of PDB 5can Chain A

Receptor sequence
>5canA (length=301) Species: 9606 (Homo sapiens) [Search protein sequence]
GEAPNQALLRILKETEFKKIKVLGSGAFGTVYKGLWIPEGEKVKIPVAIK
ELATSPKANKEILDEAYVMASVDNPHVCRLLGICLTSTVQLIMQLMPFGC
LLDYVREHKDNIGSQYLLNWCVQIAKGMNYLEDRRLVHRDLAARNVLVKT
PQHVKITDFGRAKLVPIKWMALESILHRIYTHQSDVWSYGVTVWELMTFG
SKPYDGIPASEISSILEKGERLPQPPICTIDVYMIMVKCWMIDADSRPKF
RELIIEFSKMARDPQRYLVIQGDERMHLPSPTDSNFYDMDDVVDADEYLI
P
3D structure
PDB5can Noncovalent Mutant Selective Epidermal Growth Factor Receptor Inhibitors: A Lead Optimization Case Study.
ChainA
Resolution2.8 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 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 4ZB A L718 A743 C775 M790 Q791 L792 M793 L844 T854 D855 L23 A48 C78 M93 Q94 L95 M96 L147 T157 D158 PDBbind-CN: -logKd/Ki=6.91,Ki=124nM
BindingDB: Ki=681nM
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:5can, PDBe:5can, PDBj:5can
PDBsum5can
PubMed26455919
UniProtP00533|EGFR_HUMAN Epidermal growth factor receptor (Gene Name=EGFR)

[Back to BioLiP]