1THX
THIOREDOXIN-2
Summary for 1THX
Entry DOI | 10.2210/pdb1thx/pdb |
Descriptor | THIOREDOXIN (2 entities in total) |
Functional Keywords | oxido-reductase, electron transport |
Biological source | Nostoc sp. |
Total number of polymer chains | 1 |
Total formula weight | 12811.78 |
Authors | Saarinen, M.,Gleason, F.K.,Eklund, H. (deposition date: 1995-07-07, release date: 1995-10-15, Last modification date: 2024-10-23) |
Primary citation | Saarinen, M.,Gleason, F.K.,Eklund, H. Crystal structure of thioredoxin-2 from Anabaena. Structure, 3:1097-1108, 1995 Cited by PubMed Abstract: Thioredoxins are ubiquitous proteins that serve as reducing agents and general protein disulfide reductases. The structures of thioredoxins from a number of species, including man and Escherichia coli, are known. Cyanobacteria, such as Anabaena, contain two thioredoxins that exhibit very different activities with target enzymes and share little sequence similarity. Thioredoxin-2 (Trx-2) from Anabaena resembles chloroplast type-f thioredoxin in its activities and the two proteins may be evolutionarily related. We have undertaken structural studies of Trx-2 in order to gain insights into the structure/function relationships of thioredoxins. PubMed: 8590004DOI: 10.1016/S0969-2126(01)00245-3 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.6 Å) |
Structure validation
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