PDBe 1yxs

X-ray diffraction
2.2Å resolution

Crystal Structure of Kinase Pim1 with P123M mutation

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:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Serine/threonine-protein kinase pim-1 Chain: A
Molecule details ›
Chain: A
Length: 293 amino acids
Theoretical weight: 33.87 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P11309 (Residues: 120-404; Coverage: 71%)
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: ALS BEAMLINE 8.3.1
Spacegroup: P65
Unit cell:
a: 99.315Å b: 99.315Å c: 80.561Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.197 0.195 0.237
Expression system: Escherichia coli