Structure of PDB 3byu Chain A

Receptor sequence
>3byuA (length=256) Species: 9606 (Homo sapiens) [Search protein sequence]
KPWWEDEWEVPRETLKLVERLGAGQFGEVWMGYYNGHTKVAVKSLKQGSM
SPDAFLAEANLMKQLQHQRLVRLYAVVTQEPIYIITEYMENGSLVDFLKT
PSGIKLTINKLLDMAAQIAEGMAFIEERNYIHRDLRAANILVSDTLSCKI
ADFGLKFPIKWTAPEAINYGTFTIKSDVWSFGILLTEIVTHGRIPYPGMT
NPEVIQNLERGYRMVRPDNCPEELYQLMRLCWKERPEDRPTFDYLRSVLE
DFFTAT
3D structure
PDB3byu Structure-guided design of aminopyrimidine amides as potent, selective inhibitors of lymphocyte specific kinase: synthesis, structure-activity relationships, and inhibition of in vivo T cell activation.
ChainA
Resolution2.3 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 F402
Catalytic site (residue number reindexed from 1) D134 R136 A138 N139 D152 F157
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 AM6 A A271 V272 K273 E288 M292 T316 Y318 M319 G322 L371 A381 D382 F383 A41 V42 K43 E58 M62 T86 Y88 M89 G92 L141 A151 D152 F153 MOAD: ic50=0.8nM
PDBbind-CN: -logKd/Ki=9.10,IC50=0.8nM
BindingDB: IC50=0.8nM
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

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Molecular Function
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Biological Process
External links
PDB RCSB:3byu, PDBe:3byu, PDBj:3byu
PDBsum3byu
PubMed18321037
UniProtP06239|LCK_HUMAN Tyrosine-protein kinase Lck (Gene Name=LCK)

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