PDBe 3ma3

X-ray diffraction
2.3Å resolution

Crystal structure of human proto-oncogene serine threonine kinase (PIM1) in complex with a consensus peptide and a naphtho-difuran 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):
Pimtide Chain: B
Molecule details ›
Chain: B
Length: 7 amino acids
Theoretical weight: 941 Da
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: 35.67 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P11309 (Residues: 93-403; Coverage: 77%)
Gene name: PIM1
Sequence domains: Protein kinase domain
Structure domains:

Ligands and Environments

1 bound ligand:

1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU FR-E SUPERBRIGHT
Spacegroup: P65
Unit cell:
a: 97.707Å b: 97.707Å c: 80.581Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.172 0.169 0.233
Expression systems:
  • Not provided
  • Escherichia coli BL21(DE3)