› 2o3p

X-ray diffraction
2.24Å resolution

Crystal structure of Pim1 with Quercetin

Released:
DOI: 10.2210/pdb2o3p/pdb
PDB entry 2o3p coloured by chain, front view.
PDB entry 2o3p coloured by chain, side view.
PDB entry 2o3p coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Characterization of a potent and selective small-molecule inhibitor of the PIM1 kinase.
Holder S, Zemskova M, Zhang C, Tabrizizad M, Bremer R, Neidigh JW, Lilly MB
Mol Cancer Ther 6 163-72 (2007)
PMID: 17218638

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: 293 amino acids
Theoretical weight: 33.83 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

2 bound ligands:
Ligand IMD 2 x IMD
Ligand QUE 1 x QUE
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 8.3.1
Spacegroup: P65
Unit cell:
a: 97.761Å b: 97.761Å c: 81.185Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.189 0.187 0.22
Expression system: Escherichia coli

Quick links

Citations

25 review citations

Plant polyphenols: chemical properties, biological activities, and synthesis.
Quideau et al. (2011)
24 more

13 mentions without citation

Prospects for circumventing aminoglycoside kinase mediated antibiotic resistance.
Shi et al. (2013)
12 more