› 4dtk

X-ray diffraction
1.86Å resolution

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: 276 amino acids
Theoretical weight: 31.91 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P11309 (Residues: 30-305; Coverage: 88%)
Gene name: PIM1
Sequence domains: Protein kinase domain
Structure domains:

Ligands and Environments

3 bound ligands:
Ligand EDO 7 x EDO
Ligand 7LI 1 x 7LI
Ligand SO4 2 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 17-ID
Spacegroup: P65
Unit cell:
a: 97.444Å b: 97.444Å c: 81.363Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.166 0.165 0.182
Expression system: Escherichia coli

Quick links

Citations

7 review citations

Pim kinases in hematological malignancies: where are we now and where are we going?
Mondello et al. (2014)
6 more

7 mentions 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)
6 more