› 3a99

X-ray diffraction
1.6Å resolution

Structure of PIM-1 kinase crystallized in the presence of P27KIP1 Carboxy-terminal peptide

Released:
DOI: 10.2210/pdb3a99/pdb
PDB entry 3a99 coloured by chain, front view.
PDB entry 3a99 coloured by chain, side view.
PDB entry 3a99 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Cell-permeable carboxyl-terminal p27(Kip1) peptide exhibits anti-tumor activity by inhibiting Pim-1 kinase.
Morishita D, Takami M, Yoshikawa S, Katayama R, Sato S, Kukimoto-Niino M, Umehara T, Shirouzu M, Sekimizu K, Yokoyama S, Fujita N
J Biol Chem 286 2681-8 (2011)
PMID: 21062737

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-145753 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Serine/threonine-protein kinase pim-1 Chain: A
Molecule details ›
Chain: A
Length: 320 amino acids
Theoretical weight: 36.48 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P11309 (Residues: 15-313; Coverage: 96%)
Gene name: PIM1
Sequence domains: Protein kinase domain
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand MG 1 x MG
Ligand ANP 1 x ANP
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL26B2
Spacegroup: P65
Unit cell:
a: 98.156Å b: 98.156Å c: 80.296Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.187 0.187 0.206
Expression system: Escherichia coli

Quick links

Citations

6 review citations

PIM Kinase as an Executional Target in Cancer.
Zhang et al. (2018)
5 more

9 mentions without citation

A water-mediated allosteric network governs activation of Aurora kinase A.
Cyphers et al. (2017)
8 more