BioLiP

Structure of PDB 2e2b Chain B

Receptor sequence

>2e2bB (length=262) Species: 9606 (Homo sapiens) [Search protein sequence]

MDPSSPNYDKWEMERTDITMKHKLGGGQYGEVYEGVWKKYSLTVAVKTLE
VEEFLKEAAVMKEIKHPNLVQLLGVCTREPPFYIITEFMTYGNLLDYLRE
CNRQEVNAVVLLYMATQISSAMEYLEKKNFIHRDLAARNCLVGENHLVKV
ADFGLSTYTAHAGAKFPIKWTAPESLAYNKFSIKSDVWAFGVLLWEIATY
GMSPYPGIDLSQVYELLEKDYRMERPEGCPEKVYELMRACWQWNPSDRPS
FAEIHQAFETMF

3D structure

PDB

2e2b Structural factors contributing to the Abl/Lyn dual inhibitory activity of 3-substituted benzamide derivatives

Chain

Resolution

2.2 Å

3D
structure

Catalytic site residues are labeled in the structure
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Enzymatic activity

Catalytic site (original residue number in PDB)	D363 A365 R367 N368 D381 P402
Catalytic site (residue number reindexed from 1)	D134 A136 R138 N139 D152 P167
Enzyme Commision number	2.7.10.2: non-specific 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	406	B	L248 Y253 V256 A269 K271 E286 V289 M290 L298 I313 T315 F317 M318 I360 H361 R362 A380 D381 F382	L24 Y29 V32 A45 K47 E57 V60 M61 L69 I84 T86 F88 M89 I131 H132 R133 A151 D152 F153	MOAD: ic50=11nM BindingDB: IC50=4.0nM

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

PDB	RCSB:2e2b, PDBe:2e2b, PDBj:2e2b
PDBsum	2e2b
PubMed	17376680
UniProt	P00519\|ABL1_HUMAN Tyrosine-protein kinase ABL1 (Gene Name=ABL1)