PDBe 3qf9

X-ray diffraction
2.2Å resolution

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

Released:
Entry authors: Filippakopoulos P, Bullock AN, Fedorov O, Miduturu CV, von Delft F, Arrowsmith CH, Weigelt J, Edwards A, Bountra C, Grey N, Knapp S, Structural Genomics Consortium (SGC)

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 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

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: 97.843Å b: 97.843Å c: 80.428Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.188 0.186 0.227
Expression systems:
  • Not provided
  • Escherichia coli BL21(DE3)