PyDISH

PyDISH analyzes over 13,000 heme structures from the Protein Data Bank (PDB) to quantify porphyrin distortion, axial ligand coordination, propionate sidechain orientation, and associated protein structural features for comparative and functional studies.

Key Features:

• Heme Structure Database: Curates >13,000 PDB-derived heme structures with annotated porphyrin distortion parameters, axial ligands, coordination distances, and propionate sidechain orientations.
• Integrated Structural Annotation: Links heme entries to protein domains, UniProt IDs, CATH fold classifications, organism metadata, and structural measurements.
• Statistical Structural Analysis: Performs quantitative analysis of heme porphyrin geometries and coordination features to identify structural trends across heme proteins.
• Functional Correlation Analysis: Evaluates relationships between porphyrin distortion and biological functions including oxygen transport, electron transfer, and transcriptional regulation.

Scientific Applications:

• Heme Protein Functional Analysis: Investigates structural determinants of functional diversity and supports hypothesis generation and protein design based on heme geometry and coordination patterns.

Methodology:

PyDISH systematically integrates Protein Data Bank (PDB) structural data with quantitative analysis of heme porphyrin distortion and coordination geometry to correlate structural parameters with functional properties of heme proteins.