PDBe 3cy2

X-ray diffraction
2.01Å resolution

Crystal structure of human proto-oncogene serine threonine kinase (PIM1) in complex with a consensus peptide and a beta carboline ligand II

Released:

Function and Biology Details

Reaction catalysed:
ATP + a protein = ADP + a phosphoprotein. 
Biochemical function:
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Pimtide peptide Chain: B
Molecule details ›
Chain: B
Length: 14 amino acids
Theoretical weight: 1.59 KDa
Source organism: Synthetic construct
Expression system: Not provided
Serine/threonine-protein kinase pim-1 Chain: A
Molecule details ›
Chain: A
Length: 314 amino acids
Theoretical weight: 35.72 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P11309 (Residues: 92-404; Coverage: 78%)
Gene name: PIM1
Sequence domains: Protein kinase domain
Structure domains:

Ligands and Environments

3 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU FR-E+ SUPERBRIGHT
Spacegroup: P65
Unit cell:
a: 98.668Å b: 98.668Å c: 81.129Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.169 0.167 0.199
Expression systems:
  • Not provided
  • Escherichia coli