Structure of PDB 2jiv Chain B

Receptor sequence
>2jivB (length=272) Species: 9606 (Homo sapiens) [Search protein sequence]
PNQALLRILKETEFKKIKVLGSGAFGTVYKGLWIPEGEKVKIPVAIKELR
EATSPANKEILDEAYVMASVDNPHVCRLLGICLTSTVQLIMQLMPFGCLL
DYVREHKDNIGSQYLLNWCVQIAKGMNYLEDRRLVHRDLAARNVLVKTPQ
HVKITDFGLAKLGGKVPIKWMALESILHRIYTHQSDVWSYGVTVWELMTF
GSKPYDGIPASEISSILEKGERLPQPPICTIDVYMIMVKCWMIDADSRPK
FRELIIEFSKMARDPQRYLVIQ
3D structure
PDB2jiv The T790M Mutation in Egfr Kinase Causes Drug Resistance by Increasing the Affinity for ATP.
ChainB
Resolution3.5 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 G874
Catalytic site (residue number reindexed from 1) D138 A140 R142 N143 D156 G164
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 HKI B L718 A743 L788 I789 M790 P794 G796 C797 T854 D855 F856 L20 A45 L89 I90 M91 P95 G97 C98 T155 D156 F157
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:2jiv, PDBe:2jiv, PDBj:2jiv
PDBsum2jiv
PubMed18227510
UniProtP00533|EGFR_HUMAN Epidermal growth factor receptor (Gene Name=EGFR)

[Back to BioLiP]