› 5vua

X-ray diffraction
2.2Å resolution

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: B
Molecule details ›
Chain: B
Length: 298 amino acids
Theoretical weight: 34.19 KDa
Source organism: Homo sapiens
Expression system: Cell-free gateway cloning vector C-term 8xHis pCellFree_G02
UniProt:
  • Canonical: P11309 (Residues: 29-313; Coverage: 91%)
Gene name: PIM1
Sequence domains: Protein kinase domain
Structure domains:

Ligands and Environments

3 bound ligands:
Ligand GOL 1 x GOL
Ligand PO4 1 x PO4
Ligand 8GX 1 x 8GX
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL26B2
Spacegroup: P65
Unit cell:
a: 98.14Å b: 98.14Å c: 80.51Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.167 0.166 0.196
Expression system: Cell-free gateway cloning vector C-term 8xHis pCellFree_G02

Quick links

Citations

11 citation in other articles

Intermolecular interaction among Remdesivir, RNA and RNA-dependent RNA polymerase of SARS-CoV-2 analyzed by fragment molecular orbital calculation.
Kato et al. (2020)
10 more

1 mention without citation

Novel and Potential Small Molecule Scaffolds as DYRK1A Inhibitors by Integrated Molecular Docking-Based Virtual Screening and Dynamics Simulation Study.
Shahroz et al. (2022)