2bzh

X-ray diffraction
1.9Å resolution

CRYSTAL STRUCTURE OF THE HUMAN PIM1 IN COMPLEX WITH A RUTHENIUM ORGANOMETALLIC LIGAND RU1

Released:
Source organism: Homo sapiens
Entry authors: Debreczeni JE, Bullock A, Knapp S, von Delft F, Sundstrom M, Arrowsmith C, Weigelt J, Edwards A

Function and Biology Details

Reaction catalysed:
ATP + a protein = ADP + a phosphoprotein
Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Serine/threonine-protein kinase pim-1 Chain: B
Molecule details ›
Chain: B
Length: 313 amino acids
Theoretical weight: 35.63 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: P11309 (Residues: 1-313; Coverage: 100%)
Gene name: PIM1
Structure domains:

Ligands and Environments

3 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU FR-E
Spacegroup: P65
Unit cell:
a: 97.529Å b: 97.529Å c: 80.726Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.159 0.157 0.19
Expression system: Escherichia coli BL21