1GN0
Escherichia coli GlpE sulfurtransferase soaked with KCN
Summary for 1GN0
Entry DOI | 10.2210/pdb1gn0/pdb |
Related | 1GMX |
Descriptor | THIOSULFATE SULFURTRANSFERASE GLPE, SODIUM ION, 1,2-ETHANEDIOL, ... (4 entities in total) |
Functional Keywords | transferase, rhodanese, sulfurtransferase, glycerol metabolism |
Biological source | ESCHERICHIA COLI |
Cellular location | Cytoplasm: P0A6V5 |
Total number of polymer chains | 1 |
Total formula weight | 12177.48 |
Authors | Spallarossa, A.,Donahue, J.T.,Larson, T.J.,Bolognesi, M.,Bordo, D. (deposition date: 2001-10-01, release date: 2001-11-29, Last modification date: 2024-05-08) |
Primary citation | Spallarossa, A.,Donahue, J.T.,Larson, T.J.,Bolognesi, M.,Bordo, D. Escherichia Coli Glpe is a Prototype Sulfurtransferase for the Single-Domain Rhodanese Homology Superfamily Structure, 9:1117-, 2001 Cited by PubMed Abstract: Rhodanese domains are structural modules occurring in the three major evolutionary phyla. They are found as single-domain proteins, as tandemly repeated modules in which the C-terminal domain only bears the properly structured active site, or as members of multidomain proteins. Although in vitro assays show sulfurtransferase or phosphatase activity associated with rhodanese or rhodanese-like domains, specific biological roles for most members of this homology superfamily have not been established. PubMed: 11709175DOI: 10.1016/S0969-2126(01)00666-9 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.8 Å) |
Structure validation
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