PDBe 3jpv

X-ray diffraction
2.35Å resolution

Crystal structure of human proto-oncogene serine threonine kinase (PIM1) in complex with a consensus peptide and a pyrrolo[2,3-a]carbazole ligand

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):
Peptide (PIMTIDE) ARKRRRHPSGPPTA 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: 313 amino acids
Theoretical weight: 35.59 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P11309 (Residues: 92-403; Coverage: 77%)
Gene name: PIM1
Sequence domains: Protein kinase domain
Structure domains:

Ligands and Environments

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU FR-E SUPERBRIGHT
Spacegroup: P65
Unit cell:
a: 97.821Å b: 97.821Å c: 80.743Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.176 0.173 0.226
Expression systems:
  • Not provided
  • Escherichia coli BL21(DE3)