4l67

X-ray diffraction
2.8Å resolution

Crystal Structure of Catalytic Domain of PAK4

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)
PDBe Complex ID:
PDB-CPX-132116 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Serine/threonine-protein kinase PAK 4 Chain: A
Molecule details ›
Chain: A
Length: 292 amino acids
Theoretical weight: 33.01 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: O96013 (Residues: 300-591; Coverage: 49%)
Gene names: KIAA1142, PAK4
Sequence domains: Protein kinase domain
Structure domains:
Serine/threonine-protein kinase PAK 4 Chain: B
Molecule details ›
Chain: B
Length: 25 amino acids
Theoretical weight: 2.9 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: O96013 (Residues: 36-60; Coverage: 4%)
Gene names: KIAA1142, PAK4
Sequence domains: P21-Rho-binding domain

Ligands and Environments

No bound ligands
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU FR-D
Spacegroup: P41212
Unit cell:
a: 65.175Å b: 65.175Å c: 184.567Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.233 0.228 0.333
Expression system: Escherichia coli