2HT9
The structure of dimeric human glutaredoxin 2
Summary for 2HT9
Entry DOI | 10.2210/pdb2ht9/pdb |
Descriptor | Glutaredoxin-2, 12-mer peptide, GLUTATHIONE, ... (5 entities in total) |
Functional Keywords | thioredoxin fold, iron-sulfur cluster, 2fe2s, structural genomics, structural genomics consortium, sgc, oxidoreductase |
Biological source | Homo sapiens (human) More |
Cellular location | Isoform 1: Mitochondrion. Isoform 2: Nucleus: Q9NS18 |
Total number of polymer chains | 3 |
Total formula weight | 35631.97 |
Authors | Johansson, C.,Smee, C.,Kavanagh, K.L.,Debreczeni, J.,von Delft, F.,Gileadi, O.,Arrowsmith, C.,Weigelt, J.,Edwards, A.,Sundstrom, M.,Oppermann, U.,Structural Genomics Consortium (SGC) (deposition date: 2006-07-25, release date: 2006-08-29, Last modification date: 2023-10-25) |
Primary citation | Johansson, C.,Kavanagh, K.L.,Gileadi, O.,Oppermann, U. Reversible sequestration of active site cysteines in a 2Fe-2S-bridged dimer provides a mechanism for glutaredoxin 2 regulation in human mitochondria J.Biol.Chem., 282:3077-3082, 2007 Cited by PubMed: 17121859DOI: 10.1074/jbc.M608179200 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.9 Å) |
Structure validation
Download full validation report