MTHFD Inhibitor Crystal Structures For Acute Myeloid Leukemia

Aggregating X-ray crystallography structures of novel MTHFD inhibitors, including a highly selective MTHFD2 inhibitor (compound 31) and a dual MTHFD1/2 inhibitor (compound 34). The data supports rational drug design principles for targeting one-carbon metabolism enzymes in acute myeloid leukemia (AML). The file format is PDB and the dataset size is 195.9 KB.

Use Cases

• Analyze the cocrystal structures of compounds 31 and 34 bound to MTHFD enzymes to understand hydrogen bond and hydrophobic network interactions.
• Use the PDB files of MTHFD inhibitor complexes for structure-based virtual screening to identify new potential inhibitors.
• Compare the binding poses of the dual inhibitor 34 and the reference compound DS18561882 to elucidate structural determinants of superior antiproliferative activity.

Strengths

• Includes high-resolution X-ray crystallography data for enzyme-inhibitor complexes.
• Provides structures for both a selective MTHFD2 inhibitor and a dual MTHFD1/2 inhibitor, enabling comparative analysis.
• Dataset is associated with published research demonstrating superior tumor regression in MOLM-13 xenograft models.

Limitations

• The dataset is very small in scale at 195.9 KB, indicating limited structural data.
• The data is specific to MTHFD enzymes and AML cell lines, limiting generalizability to other cancer types or targets.
• No quantitative biological activity data (e.g., IC50 values) is explicitly mentioned as being included in the dataset files.

Provenance

Source

Author Hao Lin via figshare.

Collection Method

Generated through X-ray crystallography and systematic structure-activity optimization.

Freshness

Data was last updated on March 20, 2026.