2SPT
DIFFERENCES IN THE METAL ION STRUCTURE BETWEEN SR-AND CA-PROTHROMBIN FRAGMENT 1
Summary for 2SPT
| Entry DOI | 10.2210/pdb2spt/pdb |
| Descriptor | PROTHROMBIN, 2-acetamido-2-deoxy-beta-D-glucopyranose, STRONTIUM ION, ... (4 entities in total) |
| Functional Keywords | hydrolase(serine proteinase) |
| Biological source | Bos taurus (cattle) |
| Total number of polymer chains | 1 |
| Total formula weight | 17651.35 |
| Authors | Tulinsky, A. (deposition date: 1994-02-01, release date: 1994-05-31, Last modification date: 2025-03-26) |
| Primary citation | Seshadri, T.P.,Skrzypczak-Jankun, E.,Yin, M.,Tulinsky, A. Differences in the metal ion structure between Sr- and Ca-prothrombin fragment 1. Biochemistry, 33:1087-1092, 1994 Cited by PubMed Abstract: The structure of Sr-prothrombin fragment 1 has been solved and refined by restrained least-squares methods at 2.5-A resolution to a crystallographic R value of 0.167. The protein structure is very similar to that of Ca-fragment 1. A polymeric array of five Sr2+ ions separated by about 4.0 A is buried among six gamma-carboxyglutamic acid (Gla) residues; three other Sr2+ ions interact with other Gla residues and are located further apart. One of these was not found in the Ca-fragment 1 structure. The coordination of the Sr2+ ions resembles that of Ca2+, but there are some significant differences between them. The most notable is the lack of water coordination with Sr2+ ions and two conformations for Gla 8, which change the coordination of Sr-2 and Sr-3. A hexose moiety of an oligosaccharide was located in the vicinity of Asn101 that was flexibly disordered in Ca-fragment 1. The new Sr2+ ion found may be involved in metal ion phospholipid binding interactions along with Sr-1, and Sr-7, Sr-8. PubMed: 8110739DOI: 10.1021/bi00171a006 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.5 Å) |
Structure validation
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