Structure of PDB 1yhs Chain A

Receptor sequence
>1yhsA (length=269) Species: 9606 (Homo sapiens) [Search protein sequence]
PLESQYQVGPLLGSGGFGSVYSGIRVSDNLPVAIKHVEKDRISDWGETRV
PMEVVLLKKVSSGFSGVIRLLDWFERPDSFVLILERPEPVQDLFDFITER
GALQEELARSFFWQVLEAVRHCHNCGVLHRDIKDENILIDLNRGELKLID
FGSGALLKDTVYTDFDGTRVYSPPEWIRYHRYHGRSAAVWSLGILLYDMV
CGDIPFEHDEEIIRGQVFFRQRVSSECQHLIRWCLALRPSDRPTFEEIQN
HPWMQDVLLPQETAEIHLH
3D structure
PDB1yhs Pim-1 ligand-bound structures reveal the mechanism of serine/threonine kinase inhibition by LY294002.
ChainA
Resolution2.15 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) 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 STU A L44 G45 F49 V52 A65 L120 E121 R122 V126 D128 E171 L174 I185 D186 L12 G13 F17 V20 A33 L84 E85 R86 V90 D92 E135 L138 I149 D150 MOAD: ic50=0.01uM
PDBbind-CN: -logKd/Ki=8.00,IC50=0.01uM
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

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:1yhs, PDBe:1yhs, PDBj:1yhs
PDBsum1yhs
PubMed15657054
UniProtP11309|PIM1_HUMAN Serine/threonine-protein kinase pim-1 (Gene Name=PIM1)

[Back to BioLiP]