Structure of PDB 1yi4 Chain A

Receptor sequence
>1yi4A (length=269) Species: 9606 (Homo sapiens) [Search protein sequence]
PLESQYQVGPLLGSGGFGSVYSGIRVSDNLPVAIKHVEKDRISDWGETRV
PMEVVLLKKVSSGFSGVIRLLDWFERPDSFVLILERPEPVQDLFDFITER
GALQEELARSFFWQVLEAVRHCHNCGVLHRDIKDENILIDLNRGELKLID
FGSGALLKDTVYTDFDGTRVYSPPEWIRYHRYHGRSAAVWSLGILLYDMV
CGDIPFEHDEEIIRGQVFFRQRVSSECQHLIRWCLALRPSDRPTFEEIQN
HPWMQDVLLPQETAEIHLH
3D structure
PDB1yi4 Pim-1 ligand-bound structures reveal the mechanism of serine/threonine kinase inhibition by LY294002.
ChainA
Resolution2.4 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D167 K169 N172 D186 L193 T204
Catalytic site (residue number reindexed from 1) D131 K133 N136 D150 L157 T168
Enzyme Commision number 2.7.11.1: non-specific serine/threonine protein 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 ADN A E121 D128 L174 E85 D92 L138
Gene Ontology
Molecular Function
GO:0004672 protein kinase activity
GO:0004674 protein serine/threonine kinase activity
GO:0005524 ATP binding
Biological Process
GO:0006468 protein phosphorylation
GO:0043066 negative regulation of apoptotic process

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Molecular Function
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Biological Process
External links
PDB RCSB:1yi4, PDBe:1yi4, PDBj:1yi4
PDBsum1yi4
PubMed15657054
UniProtP11309|PIM1_HUMAN Serine/threonine-protein kinase pim-1 (Gene Name=PIM1)

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