› 5o13

X-ray diffraction
2.44Å resolution

Crystal structure of PIM1 kinase in complex with small-molecule inhibitor

Released:
DOI: 10.2210/pdb5o13/pdb
PDB 5o13 coloured by chain and viewed from the front.
PDB 5o13 coloured by chain and viewed from the side.
PDB 5o13 coloured by chain and viewed from the top.
Source organism: Homo sapiens
Primary publication:
Structural analysis of PIM1 kinase complexes with ATP-competitive inhibitors.
Bogusz J, Zrubek K, Rembacz KP, Grudnik P, Golik P, Romanowska M, Wladyka B, Dubin G
Sci Rep 7 13399 (2017)
PMID: 29042609

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)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Serine/threonine-protein kinase pim-1 Chain: A
Molecule details ›
Chain: A
Length: 298 amino acids
Theoretical weight: 34.47 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P11309 (Residues: 29-313; Coverage: 91%)
Gene name: PIM1
Sequence domains: Protein kinase domain
Structure domains:

Ligands and Environments

3 bound ligands:
Ligand 9G5 1 x 9G5
Ligand IMD 1 x IMD
Ligand CL 1 x CL
2 modified residues:
Ligand CSX 1 x CSX
Ligand SEP 1 x SEP

Experiments and Validation Details

Entry percentile scores
X-ray source: BESSY BEAMLINE 14.1
Spacegroup: P65
Unit cell:
a: 96.735Å b: 96.735Å c: 81.765Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.162 0.159 0.214
Expression system: Escherichia coli

Quick links

Citations

2 review citations

A systematic review on active sites and functions of PIM-1 protein.
Zhao et al. (2022)
1 more

1 mention without citation

Structural analysis of PIM1 kinase complexes with ATP-competitive inhibitors.
Bogusz et al. (2017)