› 5vdk

X-ray diffraction
2.7Å resolution

Crystal structure of human WEE2 kinase domain in complex with MK1775

Released:
DOI: 10.2210/pdb5vdk/pdb
PDB entry 5vdk coloured by chain, front view.
PDB entry 5vdk coloured by chain, side view.
PDB entry 5vdk 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-142965 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Wee1-like protein kinase 2 Chain: A
Molecule details ›
Chain: A
Length: 297 amino acids
Theoretical weight: 33.07 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P0C1S8 (Residues: 202-492; Coverage: 51%)
Gene names: WEE1B, WEE2
Sequence domains: Protein kinase domain
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand 8X7 1 x 8X7
Ligand PO4 3 x PO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU MICROMAX-007 HF
Spacegroup: P32
Unit cell:
a: 68.81Å b: 68.81Å c: 58.04Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.228 0.225 0.284
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

7 review citations

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

6 mentions without citation

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