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restored uniprot link but edited it to the specific form of CAH
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David
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I've been looking through PDB — the Protein Data Bank — and I noticed that the protein with the most structures is human carbonic anhydrase II (UniProt: P00918), with over a thousand X-ray structures.

This seems surprising to me, as carbonic anhydrase is a zinc-containing enzyme which catalyses a really simple reaction, and doesn’t seem to be part of any key signalling pathways. In terms of relevance to disease or as a drug target, all I could find was on DrugBank was a few glaucoma drugs which have this as their target (diclofenamide, methazolamide, acetazolamide), and those are really old (60 years).

So, what is it about carbonic anhydrase that makes it so interesting? Is it that more or better drugs are needed to target it? (For what disease?) Is it that it’s a really interesting scientific model of a metalloenzyme? Or something else?

I've been looking through PDB — the Protein Data Bank — and I noticed that the protein with the most structures is carbonic anhydrase, with over a thousand X-ray structures.

This seems surprising to me, as carbonic anhydrase is a zinc-containing enzyme which catalyses a really simple reaction, and doesn’t seem to be part of any key signalling pathways. In terms of relevance to disease or as a drug target, all I could find was on DrugBank was a few glaucoma drugs which have this as their target (diclofenamide, methazolamide, acetazolamide), and those are really old (60 years).

So, what is it about carbonic anhydrase that makes it so interesting? Is it that more or better drugs are needed to target it? (For what disease?) Is it that it’s a really interesting scientific model of a metalloenzyme? Or something else?

I've been looking through PDB — the Protein Data Bank — and I noticed that the protein with the most structures is human carbonic anhydrase II (UniProt: P00918), with over a thousand X-ray structures.

This seems surprising to me, as carbonic anhydrase is a zinc-containing enzyme which catalyses a really simple reaction, and doesn’t seem to be part of any key signalling pathways. In terms of relevance to disease or as a drug target, all I could find was on DrugBank was a few glaucoma drugs which have this as their target (diclofenamide, methazolamide, acetazolamide), and those are really old (60 years).

So, what is it about carbonic anhydrase that makes it so interesting? Is it that more or better drugs are needed to target it? (For what disease?) Is it that it’s a really interesting scientific model of a metalloenzyme? Or something else?

Removed the link to CA2 as that is only one of the carbonic anhydrases in the PDB
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David
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Why isare there so many carbonic anhydrase so popularstructures in PDBthe Protein Data Bank?

I've been looking through the PDB database (rcsb.org) of protein structures— the Protein Data Bank — and I noticed that the protein with the most structures is... carbonic anhydrase? (UniProt code P00918, with over a thousand xrayX-ray structures).

This seems surprising: to me, as carbonic anhydrase is a zinc-containing enzyme which catalyzescatalyses a really simple reaction, and doesn'tdoesn’t seem to be part of any key signalling pathways. In terms of relevance to disease or as a drug target, all I could find was on DrugBank was a few glaucoma drugs which have this as their target (diclofenamide, methazolamide, acetazolamide), and those are really old (60 years).

So, what is it about carbonic anhydrase that makes it so interesting? Is it that we need more/better or better drugs thatare needed to target it? (and forFor what disease?) Is it that it'sit’s a really interesting scientific model of a metalloenzyme? Something Or something else?

Why is carbonic anhydrase so popular in PDB?

I've been looking through the PDB database (rcsb.org) of protein structures and I noticed that the protein with the most structures is... carbonic anhydrase? (UniProt code P00918, with over a thousand xray structures)

This seems surprising: carbonic anhydrase is a zinc-containing enzyme which catalyzes a really simple reaction, and doesn't seem to be part of any key signalling pathways. In terms of relevance to disease or as a drug target, all I could find was on DrugBank was a few glaucoma drugs which have this as their target (diclofenamide, methazolamide, acetazolamide), and those are really old (60 years).

So, what is it about carbonic anhydrase that makes it so interesting? Is it that we need more/better drugs that target it? (and for what disease?) Is it that it's a really interesting scientific model of a metalloenzyme? Something else?

Why are there so many carbonic anhydrase structures in the Protein Data Bank?

I've been looking through PDB — the Protein Data Bank — and I noticed that the protein with the most structures is carbonic anhydrase, with over a thousand X-ray structures.

This seems surprising to me, as carbonic anhydrase is a zinc-containing enzyme which catalyses a really simple reaction, and doesn’t seem to be part of any key signalling pathways. In terms of relevance to disease or as a drug target, all I could find was on DrugBank was a few glaucoma drugs which have this as their target (diclofenamide, methazolamide, acetazolamide), and those are really old (60 years).

So, what is it about carbonic anhydrase that makes it so interesting? Is it that more or better drugs are needed to target it? (For what disease?) Is it that it’s a really interesting scientific model of a metalloenzyme? Or something else?

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Alex I
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Why is carbonic anhydrase so popular in PDB?

I've been looking through the PDB database (rcsb.org) of protein structures and I noticed that the protein with the most structures is... carbonic anhydrase? (UniProt code P00918, with over a thousand xray structures)

This seems surprising: carbonic anhydrase is a zinc-containing enzyme which catalyzes a really simple reaction, and doesn't seem to be part of any key signalling pathways. In terms of relevance to disease or as a drug target, all I could find was on DrugBank was a few glaucoma drugs which have this as their target (diclofenamide, methazolamide, acetazolamide), and those are really old (60 years).

So, what is it about carbonic anhydrase that makes it so interesting? Is it that we need more/better drugs that target it? (and for what disease?) Is it that it's a really interesting scientific model of a metalloenzyme? Something else?