I tried looking up some interesting enzymes involved in various industrial approaches to carbon capture and sequestration. AlphaFold has uploaded a lot of thes

I tried looking up some interesting enzymes involved in various industrial approaches to carbon capture and sequestration. AlphaFold has uploaded a lot of these to the UniProt database. Compare and contrast, for a carbonic anhydrase enzyme (catalyzes the H2O + CO2 <-> H3CO- + H+ reaction in a thermophilic bacterium): X-ray crystal structure uploaded to UniProt database (this is a trimer, i.e. the crystal unit contains 3 copies of the protein, while the AlphaFold model is the single protein): https://www.uniprot.org/uniprotkb/P40881/entry#structure https://www.uniprot.org/uniprotkb/P40881/entry#structure AlphaFold result uploaded to UniProt database: https://www.uniprot.org/uniprotkb/A0A1I6ZV33/entry#structure https://www.uniprot.org/uniprotkb/A0A1I6ZV33/entry#structure One thing to notice is that the X-ray data (structure from 2000) contains a lot more information than the Alpha model, such as location of the metal-binding active site. There's also a fair amount of uncertainty about one of the helix elements in the AlphaFold model. However, structural protein biochemistry is a very complicated field. Take a look at this (full open access) paper as an example, which uses a variety of modern computational techniques: "(2021) In Silico Investigation of Potential Applications of Gamma Carbonic Anhydrases as Catalysts of CO2 Biomineralization Processes: A Visit to the Thermophilic Bacteria Persephonella hydrogeniphila, Persephonella marina, Thermosulfidibacter takaii, and Thermus thermophilus" https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8000050/ https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8000050/ > "All γ-CAs are structurally similar, adopting a homo-trimeric architecture dominated by β-sheets and an α-helical C-terminal. These CAs are only functional in their trimeric form because each active site is located between two monomers, with two coordinating residues coming from one monomer and the third from the neighboring one." I'm guessing AlphaFold will be used more as a primary tool for getting a rough idea of the structure of unknown sequences and that X-ray crystallization and NMR dynamics methods for understanding the details, particularly when it comes to catalytic proteins, will continue to be absolutely necessary techniques, along with a wide variety of other computational techniques like molecular dynamics simulations, etc.