› 5v5y

X-ray diffraction
1.9Å resolution

CRYSTAL STRUCTURE OF HUMAN WEE1 KINASE DOMAIN IN COMPLEX WITH MK1775

Released:
DOI: 10.2210/pdb5v5y/pdb
PDB entry 5v5y coloured by chain, front view.
PDB entry 5v5y coloured by chain, side view.
PDB entry 5v5y coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structural Basis of Wee Kinases Functionality and Inactivation by Diverse Small Molecule Inhibitors.
Zhu JY, Cuellar RA, Berndt N, Lee HE, Olesen SH, Martin MP, Jensen JT, Georg GI, Schönbrunn E
J Med Chem 60 7863-7875 (2017)
PMID: 28792760

Function and Biology Details

Reaction catalysed: 
ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-151698 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Wee1-like protein kinase Chain: A
Molecule details ›
Chain: A
Length: 289 amino acids
Theoretical weight: 32.44 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P30291 (Residues: 291-575; Coverage: 44%)
Gene name: WEE1
Sequence domains: Protein kinase domain
Structure domains:

Ligands and Environments

3 bound ligands:
Ligand 8X7 1 x 8X7
Ligand DMS 2 x DMS
Ligand EDO 2 x EDO
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 22-ID
Spacegroup: P212121
Unit cell:
a: 50.08Å b: 63.1Å c: 82.46Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.173 0.171 0.215
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

6 review citations

A WEE1 family business: regulation of mitosis, cancer progression, and therapeutic target.
Ghelli Luserna di Rorà et al. (2020)
5 more

6 mentions without citation

Regulation of G2/M Transition by Inhibition of WEE1 and PKMYT1 Kinases.
Schmidt et al. (2017)
5 more