1QMV

thioredoxin peroxidase B from red blood cells

Summary for 1QMV

• Entry DOI: 10.2210/pdb1qmv/pdb
• Descriptor: PEROXIREDOXIN-2 (2 entities in total)
• Functional Keywords: sulphinic acid, thioredoxin, oxidoreductase
• Biological source: HOMO SAPIENS (HUMAN)
• Total number of polymer chains: 10
• Total formula weight: 218627.15

Authors

Isupov, M.N.,Littlechild, J.A.,Lebedev, A.A.,Errington, N.,Vagin, A.A.,Schroder, E. (deposition date: 1999-10-07, release date: 2000-07-28, Last modification date: 2024-10-23)

Primary citation

Schroder, E.,Littlechild, J.A.,Lebedev, A.A.,Errington, N.,Vagin, A.A.,Isupov, M.N.
Crystal Structure of Decameric 2-Cys Peroxiredoxin from Human Erythrocytes at 1.7 A Resolution.
Structure, 8:605-, 2000

PubMed Abstract: The peroxiredoxins (Prxs) are an emerging family of multifunctional enzymes that exhibit peroxidase activity in vitro, and in vivo participate in a range of cellular processes known to be sensitive to reactive oxygen species. Thioredoxin peroxidase B (TPx-B), a 2-Cys type II Prx from erythrocytes, promotes potassium efflux and down-regulates apoptosis and the recruitment of monocytes by endothelial tissue.

PubMed: 10873855
DOI: 10.1016/S0969-2126(00)00147-7

Experimental method

X-RAY DIFFRACTION (1.7 Å)