Structure of PDB 2rfe Chain B

Receptor sequence
>2rfeB (length=273) Species: 9606 (Homo sapiens) [Search protein sequence]
LLRILKETEFKKIKVLGSGAFGTVYKGLWIPEGEKVKIPVAIKELREATS
PKANKEILDEAYVMASVDNPHVCRLLGICLTSTVQLITQLMPFGCLLDYV
REHKDNIGSQYLLNWCVQIAEGMNYLEDRRLVHRDLAARNVLVKTPQHVK
ITDFGLAKLLGKVPIKWMALESILHRIYTHQSDVWSYGVTVWELMTFGSK
PYDGIPASEISSILEKGERLPQPPICTIDVYMIMVKCWMIDADSRPKFRE
LIIEFSKMARDPQRYLVIQGVVD
3D structure
PDB2rfe Inhibition of the EGF receptor by binding of MIG6 to an activating kinase domain interface.
ChainB
Resolution2.9 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) D813 A815 R817 N818 D831
Catalytic site (residue number reindexed from 1) D135 A137 R139 N140 D153
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 peptide B E904 G906 E907 R908 P910 Q911 P912 P913 C915 T916 I917 Y920 V924 M928 I929 V956 E215 G217 E218 R219 P221 Q222 P223 P224 C226 T227 I228 Y231 V235 M239 I240 V267
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:2rfe, PDBe:2rfe, PDBj:2rfe
PDBsum2rfe
PubMed18046415
UniProtP00533|EGFR_HUMAN Epidermal growth factor receptor (Gene Name=EGFR)

[Back to BioLiP]