› 5ime

X-ray diffraction
2.22Å resolution

Function and Biology Details

Reaction catalysed: 
ATP + a protein = ADP + a phosphoprotein
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-171568 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Serine/threonine-protein kinase PAK 1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 300 amino acids
Theoretical weight: 33.54 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q13153 (Residues: 249-545; Coverage: 55%)
Gene name: PAK1
Sequence domains: Protein kinase domain
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand 6BZ 2 x 6BZ
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRF BEAMLINE BL17U
Spacegroup: P21
Unit cell:
a: 60.48Å b: 82.82Å c: 65.89Å
α: 90° β: 106.71° γ: 90°
R-values:
R R work R free
0.226 0.224 0.263
Expression system: Escherichia coli

Quick links

Citations

11 review citations

Paving the Rho in cancer metastasis: Rho GTPases and beyond.
Jansen et al. (2018)
10 more

2 mentions without citation

Molecular modelling approaches predicted 1,2,3-triazolyl ester of ketorolac (15K) to be a novel allosteric modulator of the oncogenic kinase PAK1.
Shahinozzaman et al. (2021)
1 more