5vef

X-ray diffraction
1.75Å resolution

PAK4 kinase domain in complex with fasudil

Released:
Source organism: Homo sapiens
Primary publication:
PAK4 crystal structures suggest unusual kinase conformational movements.
Biochim. Biophys. Acta (2017)
PMID: 28993291

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 PAK 4 Chain: A
Molecule details ›
Chain: A
Length: 319 amino acids
Theoretical weight: 36.03 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: O96013 (Residues: 286-591; Coverage: 52%)
Gene names: KIAA1142, PAK4
Sequence domains: Protein kinase domain

Ligands and Environments

2 bound ligands:

1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 24-ID-E
Spacegroup: P41212
Unit cell:
a: 61.94Å b: 61.94Å c: 182.741Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.202 0.2 0.239
Expression system: Escherichia coli BL21(DE3)