Conserved Protein Domain Family
Cupredoxin

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cl19115: Cupredoxin Superfamily (this model, PSSM-Id:418529 is obsolete and has been replaced by 473140)
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Cupredoxin superfamily
Cupredoxins contain type I copper centers and are involved in inter-molecular electron transfer reactions. Cupredoxins are blue copper proteins, having an intense blue color due to the presence of a mononuclear type 1 (T1) copper site. Structurally, the cupredoxin-like fold consists of a beta-sandwich with 7 strands in 2 beta-sheets, which is arranged in a Greek-key beta-barrel. Some of these proteins have lost the ability to bind copper. The majority of family members contain multiple cupredoxin domain repeats: ceruloplasmin and the coagulation factors V/VIII have six repeats; laccase, ascorbate oxidase, spore coat protein A, and multicopper oxidase CueO contain three repeats; and nitrite reductase has two repeats. Others are mono-domain cupredoxins, such as plastocyanin, pseudoazurin, plantacyanin, azurin, rusticyanin, stellacyanin, quinol oxidase, and the periplasmic domain of cytochrome c oxidase subunit II.
Links
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Taxonomy: root
PubMed: 234 links
Protein: Related Protein
Related Structure
Statistics
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Accession: cl19115
PSSM Id: 418529
Name: Cupredoxin
Created: 16-Jan-2014
Updated: 24-Nov-2020
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