› 1yi3

X-ray diffraction
2.5Å resolution

Crystal Structure of Pim-1 bound to LY294002

Released:
DOI: 10.2210/pdb1yi3/pdb
PDB entry 1yi3 coloured by chain, front view.
PDB entry 1yi3 coloured by chain, side view.
PDB entry 1yi3 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Pim-1 ligand-bound structures reveal the mechanism of serine/threonine kinase inhibition by LY294002.
Jacobs MD, Black J, Futer O, Swenson L, Hare B, Fleming M, Saxena K
J Biol Chem 280 13728-34 (2005)
PMID: 15657054

Function and Biology Details

Reaction catalysed: 
ATP + a protein = ADP + a phosphoprotein
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-145753 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Serine/threonine-protein kinase pim-1 Chain: A
Molecule details ›
Chain: A
Length: 273 amino acids
Theoretical weight: 31.67 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P11309 (Residues: 33-305; Coverage: 87%)
Gene name: PIM1
Sequence domains: Protein kinase domain
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand LY2 1 x LY2
2 modified residues:
Ligand CME 1 x CME
Ligand SEP 1 x SEP

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: P65
Unit cell:
a: 97.647Å b: 97.647Å c: 80.725Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.208 0.208 0.259
Expression system: Escherichia coli

Quick links

Citations

30 review citations

Fuel feeds function: energy metabolism and the T-cell response.
Fox et al. (2005)
29 more

2 mentions without citation

Binding of protein kinase inhibitors to synapsin I inferred from pair-wise binding site similarity measurements.
Defranchi et al. (2010)
1 more