1WVO
Solution structure of RSGI RUH-029, an antifreeze protein like domain in human N-acetylneuraminic acid phosphate synthase gene.
Summary for 1WVO
| Entry DOI | 10.2210/pdb1wvo/pdb |
| Descriptor | Sialic acid synthase (1 entity in total) |
| Functional Keywords | antifreeze protein like domain, n-acetylneuraminic acid phosphate synthase, structural genomics, nppsfa, national project on protein structural and functional analyses, riken structural genomics/proteomics initiative, rsgi, transferase |
| Biological source | Homo sapiens (human) |
| Total number of polymer chains | 1 |
| Total formula weight | 8269.43 |
| Authors | Ito, Y.,Hamada, T.,Hayashi, F.,Yokoyama, S.,Hirota, H.,RIKEN Structural Genomics/Proteomics Initiative (RSGI) (deposition date: 2004-12-22, release date: 2006-01-03, Last modification date: 2024-05-29) |
| Primary citation | Hamada, T.,Ito, Y.,Abe, T.,Hayashi, F.,Guntert, P.,Inoue, M.,Kigawa, T.,Terada, T.,Shirouzu, M.,Yoshida, M.,Tanaka, A.,Sugano, S.,Yokoyama, S.,Hirota, H. Solution structure of the antifreeze-like domain of human sialic acid synthase Protein Sci., 15:1010-1016, 2006 Cited by PubMed Abstract: The structure of the C-terminal antifreeze-like (AFL) domain of human sialic acid synthase was determined by NMR spectroscopy. The structure comprises one alpha- and two single-turn 3(10)-helices and two beta-strands, and is similar to those of the type III antifreeze proteins. Evolutionary trace analyses of the type III antifreeze protein family suggested that the class-specific residues in the human and bacterial AFL domains are important for their substrate binding, while the class-specific residues of the fish antifreeze proteins are gathered on the ice-binding surface. PubMed: 16597820DOI: 10.1110/ps.051700406 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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