PDBe 4otg

X-ray diffraction
2.6Å resolution

Crystal Structure of PRK1 Catalytic Domain in Complex with Lestaurtinib

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 N1 Chain: A
Molecule details ›
Chain: A
Length: 341 amino acids
Theoretical weight: 38.34 KDa
Source organism: Homo sapiens
Expression system: Trichoplusia ni
UniProt:
  • Canonical: Q16512 (Residues: 605-942; Coverage: 36%)
Gene names: PAK1, PKN, PKN1, PRK1, PRKCL1
Sequence domains:
Structure domains:

Ligands and Environments

1 bound ligand:

2 modified residues:

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 21-ID-G
Spacegroup: P212121
Unit cell:
a: 56.453Å b: 73.292Å c: 94.512Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.212 0.209 0.268
Expression system: Trichoplusia ni