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Molecular Models02:00

Molecular Models

Physical models representing molecular architectures of chemical compounds play essential roles in understanding chemistry. The use of molecular models makes it easier to visualize the structures and shapes of atoms and molecules.
Protein Organization01:24

Protein Organization

Proteins are polymers of amino acid residues. They are versatile and responsible for different cellular functions, including DNA replication, molecular transport, catalysis, and structural support. Proteins have a hierarchical structure comprising at least three levels of organization: primary, secondary, and tertiary structure. Some large proteins have a quaternary structure where individual protein subunits are linked together.
The primary structure of a protein is its amino acid sequence.
Gene Families01:57

Gene Families

Gene families consist of groups of genes proposed to have originated from a common ancestor. Typically these arise through events in which a gene or genes are mistakenly duplicated during cell division. Unlike their parent genes (which are subject to selection pressure to maintain function), these gene copies do not need to preserve their sequences and may evolve at a relatively faster rate.
Occasionally these regions can be adapted to take on new roles within the organism, becoming novel genes...
Protein and Protein Structure02:15

Protein and Protein Structure

Proteins are one of the most abundant organic molecules in living systems and have the most diverse range of functions of all macromolecules. Proteins may be structural, regulatory, contractile, or protective. They may serve in transport, storage, or membranes; or they may be toxins or enzymes. Their structures, like their functions, vary greatly. They are all, however, amino acid polymers arranged in a linear sequence.
A protein's shape is critical to its function. For example, an enzyme can...

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Interdomain compactization in human tyrosyl-tRNA synthetase studied by the hierarchical rotations technique.

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Related Experiment Video

Updated: Jul 18, 2026

Modeling an Enzyme Active Site using Molecular Visualization Freeware
14:37

Modeling an Enzyme Active Site using Molecular Visualization Freeware

Published on: December 25, 2021

[Computer modeling of cytochrome P450 2E1 three-dimensional structure].

I M Danko, K A Odynets, V O Kitam

    Ukrains'Kyi Biokhimichnyi Zhurnal (1999 )
    |November 15, 2006
    PubMed
    Summary

    This study models the human cytochrome P450 2E1 (CYP2E1) structure, revealing distinct active site features compared to related enzymes. Understanding CYP2E1 active site characteristics is crucial for drug metabolism research.

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    Related Experiment Videos

    Last Updated: Jul 18, 2026

    Modeling an Enzyme Active Site using Molecular Visualization Freeware
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    Published on: December 25, 2021

    Modeling Ligands into Maps Derived from Electron Cryomicroscopy
    09:30

    Modeling Ligands into Maps Derived from Electron Cryomicroscopy

    Published on: July 19, 2024

    Unraveling Entropic Rate Acceleration Induced by Solvent Dynamics in Membrane Enzymes
    09:42

    Unraveling Entropic Rate Acceleration Induced by Solvent Dynamics in Membrane Enzymes

    Published on: January 16, 2016

    Area of Science:

    • Biochemistry
    • Computational Biology
    • Structural Biology

    Context:

    • Cytochrome P450 enzymes, particularly CYP2E1, play a vital role in drug metabolism and detoxification.
    • Understanding the three-dimensional structure of CYP2E1 is essential for predicting substrate interactions and enzyme activity.
    • Homology modeling provides a valuable approach to elucidate enzyme structures when experimental data is limited.

    Purpose:

    • To construct a detailed three-dimensional computer model of human cytochrome P450 2E1 (CYP2E1).
    • To analyze and compare the active site characteristics of CYP2E1 with those of CYP2C5 and CYP2C9.
    • To identify key amino acid residues and structural features within the CYP2E1 active site.

    Summary:

    • A homology model of human CYP2E1 was developed using crystallographic data from CYP2C5 and CYP2C9.
    • Significant secondary structure homology was observed across different species for CYP2E1.
    • The model established the heme location and identified distinct differences in active site pocket size and amino acid composition between CYP2E1, CYP2C5, and CYP2C9.

    Impact:

    • Provides a structural basis for understanding CYP2E1's role in xenobiotic metabolism.
    • Facilitates the design of targeted inhibitors or activators for CYP2E1.
    • Contributes to the broader understanding of cytochrome P450 enzyme diversity and function.