› 5vcz

X-ray diffraction
1.5Å resolution

CRYSTAL STRUCTURE OF HUMAN MYT1 KINASE DOMAIN IN COMPLEX WITH Bosutinib isomer

Released:
DOI: 10.2210/pdb5vcz/pdb
PDB entry 5vcz coloured by chain, front view.
PDB entry 5vcz coloured by chain, side view.
PDB entry 5vcz 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 = ADP + a phosphoprotein
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-189237 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Membrane-associated tyrosine- and threonine-specific cdc2-inhibitory kinase Chain: A
Molecule details ›
Chain: A
Length: 311 amino acids
Theoretical weight: 34.5 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q99640 (Residues: 75-362; Coverage: 58%)
Gene names: MYT1, PKMYT1
Sequence domains: Protein kinase domain

Ligands and Environments

3 bound ligands:
Ligand XZN 1 x XZN
Ligand EDO 5 x EDO
Ligand PEG 1 x PEG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 22-ID
Spacegroup: P212121
Unit cell:
a: 46.63Å b: 54.97Å c: 113.53Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.148 0.148 0.181
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

2 mentions without citation

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