The Fascinating World of 7dak: A Serotonin N-Acetyltransferase’s Tale

Henry Gibson


The study of proteins and enzymes is vital to the advancement of molecular biology and structural biology, which in turn advances our understanding of life at the molecular level. Oryza Sativa, more popularly known as rice, contains a protein called 7dak, a serotonin N-acetyltransferase, that has piqued the curiosity of scientists. Intriguing new insights into the function of this unique protein are revealed upon complexation with 5-Methoxytryptamine and acetyl-CoA. To better understand the role of 7DAK in biology, we shall examine its crystal structure, discuss its classification, its organism of origin, and much more in the following sections.

Unraveling 7DAK: An In-Depth Exploration

·       The Crystal Structure

The crystal structure of 7DAK illustrates the structure of the molecule in three dimensions. Understanding its function and interactions with other molecules requires knowing its structure.

·       The Complex Formation

The relationship between 7DAK, 5-Methoxytryptamine, and acetyl-CoA is intriguing. Melatonin production relies heavily on the development of this complex.

·       Classification: TRANSFERASE

7DAK is categorized as a “TRANSFERASE,” which indicates that it catalyzes the transfer of functional groups between molecules. This is an essential mechanism in many biological reactions.

·       Organism of Origin

7DAK originates from the rice species Oryza Sativa. Learning about a species’ ancestry is crucial to any investigation into its development and adaptations.

·       Expression System

The bacterial expression system Escherichia coli BL21(DE3) is widely used in laboratories to produce recombinant proteins, including 7DAK.

·       Mutation Status

Notably, no mutations in 7DAK have been identified, making it a prime candidate for structural and functional analyses.

·       Deposition and Release

On October 16, 2020, the structural data for 7DAK was submitted, and on September 22, 2021, it was published, making it available for study.

The X-Ray Diffraction Method

·       Method: X-RAY DIFFRACTION

To determine 7DAK’s crystal structure, X-ray diffraction is utilized. By beaming X-rays on the crystal, a diffraction pattern is produced that shows the atomic arrangement.

·       Resolution: 2.80 Å

The crystal structure is highly resolved, as shown by a resolution of 2.80 ngstroms. Higher resolution and more distinct understanding correspond to smaller ngstrom values.

·       R-Values

R-values represent measures of the structural model’s reliability. A well-fitting model is shown by R-Values of 0.266 for the free data, 0.200 for the worked data, and 0.207 for the observed data in the instance of 7DAK.

Ligand Structure Quality Assessment

·       Ligand Structure Quality

The quality of ligand structures in the complex is essential for understanding how 7DAK interacts with 5-Methoxytryptamine and acetyl-CoA. A well-fitted ligand structure ensures the accuracy of the complex.

·       Literature Insights

To further understand the catalytic mechanism of 7DAK during melatonin production, a study named “Structural and Molecular Dynamics Analysis of Plant Serotonin N-Acetyltransferase” by Liao, L., Zhou, Y., and others was published in Angewandte Chemie International Edition in 2021.

·       PubMed Abstract

PubMed is a widely used database for scientific literature and it also contains the research on 7DAK. Researchers would do well to consult this abstract in their pursuit of a deeper knowledge of 7DAK.

Biological Assembly and Macromolecule Content

·       Biological Assembly

C2 cyclic symmetry can be seen in the biological assembly formed by 7’DAK. Its purpose can only be grasped through an appreciation of its biological construction.

·       Macromolecule Details

Researchers can better understand the intricacy of 7’DAK and the roles it plays in biological processes because to the information provided on its mass, number of atoms, and individual protein chains.


Oryza sativa serotonin N-acetyltransferase (7DAK) is a key enzyme in melatonin production, as stated previously. Researchers can learn a lot from studying its crystal structure, expression system, and ligand interactions. The discovery of this amazing enzyme has paved the way for new understandings in molecular biology.

Read More:


What is the role of 7DAK in melatonin biosynthesis?

Melatonin is an essential chemical with several physiological effects, and 7’DAK is a critical enzyme in its production.

Why is the crystal structure of 7DAK important?

By showing how the atoms in 7’DAK are arranged in three dimensions, the crystal structure sheds light on the protein’s function and relationships.

How does 7DAK interact with 5-Methoxytryptamine and acetyl-CoA?

Essential to its function in melatonin biosynthesis is the interaction of 7’DAK with 5-Methoxytryptamine and acetyl-CoA.

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