Structure of PDB 2pl0 Chain A

Receptor sequence
>2pl0A (length=268) Species: 9606 (Homo sapiens) [Search protein sequence]
KPWWEDEWEVPRETLKLVERLGAGQFGEVWMGYYNGHTKVAVKSLKQGSM
SPDAFLAEANLMKQLQHQRLVRLYAVVTQEPIYIITEYMENGSLVDFLKT
PSGIKLTINKLLDMAAQIAEGMAFIEERNYIHRDLRAANILVSDTLSCKI
ADFGLARLIEDNEYTAREGAKFPIKWTAPEAINYGTFTIKSDVWSFGILL
TEIVTHGRIPYPGMTNPEVIQNLERGYRMVRPDNCPEELYQLMRLCWKER
PEDRPTFDYLRSVLEDFF
3D structure
PDB2pl0 Classifying protein kinase structures guides use of ligand-selectivity profiles to predict inactive conformations: Structure of lck/imatinib complex.
ChainA
Resolution2.8 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D364 R366 A368 N369 D382 A400 F402
Catalytic site (residue number reindexed from 1) D134 R136 A138 N139 D152 A170 F172
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 STI A A271 K273 E288 M292 V301 I314 T316 Y318 M319 I361 H362 A381 D382 F383 A41 K43 E58 M62 V71 I84 T86 Y88 M89 I131 H132 A151 D152 F153 PDBbind-CN: -logKd/Ki=7.21,Kd=0.062uM
BindingDB: Kd=40nM,IC50=320nM,Ki=6893nM
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:2pl0, PDBe:2pl0, PDBj:2pl0
PDBsum2pl0
PubMed17910071
UniProtP06239|LCK_HUMAN Tyrosine-protein kinase Lck (Gene Name=LCK)

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