PDBe 1f3m

X-ray diffraction
2.3Å resolution

CRYSTAL STRUCTURE OF HUMAN SERINE/THREONINE KINASE PAK1

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:
hetero tetramer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Serine/threonine-protein kinase PAK 1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 80 amino acids
Theoretical weight: 9.18 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q13153 (Residues: 70-149; Coverage: 15%)
Gene name: PAK1
Sequence domains: P21-Rho-binding domain
Structure domains: SerineThreonine-protein kinase PAK-alpha; Chain A
Serine/threonine-protein kinase PAK 1 Chains: C, D
Molecule details ›
Chains: C, D
Length: 297 amino acids
Theoretical weight: 33.27 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:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 14-BM-C
Spacegroup: P41
Unit cell:
a: 94.583Å b: 94.583Å c: 147.497Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.237 0.237 0.258
Expression system: Escherichia coli