› 2xj0

X-ray diffraction
3.1Å resolution

Protein kinase Pim-1 in complex with fragment-4 from crystallographic fragment screen

Released:
DOI: 10.2210/pdb2xj0/pdb
PDB entry 2xj0 coloured by chain, front view.
PDB entry 2xj0 coloured by chain, side view.
PDB entry 2xj0 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
A crystallographic fragment screen identifies cinnamic acid derivatives as starting points for potent Pim-1 inhibitors.
Schulz MN, Fanghänel J, Schäfer M, Badock V, Briem H, Boemer U, Nguyen D, Husemann M, Hillig RC
Acta Crystallogr D Biol Crystallogr 67 156-66 (2011)
PMID: 21358046

Function and Biology Details

Reaction catalysed: 
ATP + a protein = ADP + a phosphoprotein
Biochemical function:
Biological process:
Cellular component:
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: 301 amino acids
Theoretical weight: 34.31 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P11309 (Residues: 14-313; Coverage: 96%)
Gene name: PIM1
Sequence domains: Protein kinase domain
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand XJ0 1 x XJ0
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: BESSY BEAMLINE 14.2
Spacegroup: P65
Unit cell:
a: 96.239Å b: 96.239Å c: 80.457Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.218 0.216 0.263
Expression system: Escherichia coli

Quick links

Citations

1 review citation

Targeting Pim kinases for cancer treatment: opportunities and challenges.
Le et al. (2015)
4 other articles

1 mention without citation

Identification of the first inhibitor of the GBP1:PIM1 interaction. Implications for the development of a new class of anticancer agents against paclitaxel resistant cancer cells.
Andreoli et al. (2014)