4o38

X-ray diffraction
2.1Å resolution

Crystal structure of the human cyclin G associated kinase (GAK)

Released:
Source organism: Homo sapiens
Entry authors: Zhang R, Hatzos-Skintges C, Weger A, Chaikuad A, Eswaran J, Fedorov O, King O, von Delft F, Bountra C, Arrowsmith CH, Weigelt J, Edwards A, Knapp S, Joachimiak A, Midwest Center for Structural Genomics (MCSG), Structural Genomics Consortium (SGC)

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:
homo dimer (preferred)
PDBe Complex ID:
PDB-CPX-127252 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Cyclin-G-associated kinase Chains: A, B
Molecule details ›
Chains: A, B
Length: 338 amino acids
Theoretical weight: 38.2 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: O14976 (Residues: 12-347; Coverage: 26%)
Gene names: DNAJC26, GAK
Sequence domains: Protein kinase domain
Structure domains:

Ligands and Environments

2 bound ligands:
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-ID
Spacegroup: P3221
Unit cell:
a: 103.425Å b: 103.425Å c: 131.951Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.166 0.165 0.195
Expression system: Escherichia coli