5j0a

X-ray diffraction
2.74Å resolution

Crystal structure of PDZ-binding kinase

Released:
Source organism: Homo sapiens
Primary publication:
The crystal structure of an inactive dimer of PDZ-binding kinase.
Biochem Biophys Res Commun 476 586-593 (2016)
PMID: 27262437

Function and Biology Details

Reaction catalysed:
ATP + L-seryl/L-threonyl/L-tyrosyl-[protein] = ADP + O-phospho-L-seryl/O-phospho-L-threonyl/O-phospho-L-tyrosyl-[protein]
Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
PDBe Complex ID:
PDB-CPX-188593 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Lymphokine-activated killer T-cell-originated protein kinase Chain: A
Molecule details ›
Chain: A
Length: 300 amino acids
Theoretical weight: 33.63 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q96KB5 (Residues: 23-320; Coverage: 93%)
Gene names: PBK, TOPK
Sequence domains: Protein kinase domain
Lymphokine-activated killer T-cell-originated protein kinase Chain: B
Molecule details ›
Chain: B
Length: 304 amino acids
Theoretical weight: 34 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q96KB5 (Residues: 19-319; Coverage: 94%)
Gene names: PBK, TOPK
Sequence domains: Protein kinase domain

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRF BEAMLINE BL17U
Spacegroup: P212121
Unit cell:
a: 75.558Å b: 97.905Å c: 162.835Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.222 0.222 0.271
Expression system: Escherichia coli BL21(DE3)