› 1xqz

X-ray diffraction
2.1Å resolution

Crystal Structure of hPim-1 kinase at 2.1 A resolution

Released:
DOI: 10.2210/pdb1xqz/pdb
PDB entry 1xqz coloured by chain, front view.
PDB entry 1xqz coloured by chain, side view.
PDB entry 1xqz coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structural basis of constitutive activity and a unique nucleotide binding mode of human Pim-1 kinase.
Qian KC, Wang L, Hickey ER, Studts J, Barringer K, Peng C, Kronkaitis A, Li J, White A, Mische S, Farmer B
J Biol Chem 280 6130-7 (2005)
PMID: 15525646

Function and Biology Details

Reaction catalysed: 
ATP + a protein = ADP + a phosphoprotein
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

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: 300 amino acids
Theoretical weight: 34.25 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

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU300
Spacegroup: P65
Unit cell:
a: 95.9Å b: 95.9Å c: 79.96Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.249 0.249 0.297
Expression system: Escherichia coli

Quick links

Citations

29 review citations

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

4 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)
3 more