Differences in the metal ion structure between sr-and ca-prothrombin fragment 1. Determined by X-ray diffraction at 2.5 Å resolution. Released 31 May 1994.
Explore 2SPT in 3D Show helices and sheets RCSB PDB PDBe
2SPT contains 9 α-helices and 8 β-strands across 1 chain. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 7-9 | 3 | |
| α-helix | 14 | 1 | |
| α-helix | 15-19 | 5 | |
| α-helix | 25-32 | 8 | |
| α-helix | 36-46 | 11 | |
| α-helix | 57-63 | 7 | |
| β-strand | 67 | 1 | 1 |
| β-strand | 80 | 1 | 2 |
| β-strand | 86 | 1 | 2 |
| β-strand | 87 | 1 | 3 |
| α-helix | 88-89 | 2 | |
| β-strand | 126-128 | 3 | 4 |
| β-strand | 129 | 1 | 3 |
| β-strand | 136-138 | 3 | 4 |
| α-helix | 142 | 1 | |
| β-strand | 143 | 1 | 1 |
| α-helix | 144 | 1 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Prothrombin | A | protein | 145 | Bos taurus | P00735 (AlphaFold model) |
>2SPT_1 PROTHROMBIN (chains A) ANKGFLEEVRKGNLERECLEEPCSREEAFEALESLSATDAFWAKYTACESARNPREKLNE CLEGNCAEGVGMNYRGNVSVTRSGIECQLWRSRYPHKPEINSTTHPGADLRENFCRNPDG SITGPWCYTTSPTLRREECSVPVCG
Differences in the metal ion structure between Sr- and Ca-prothrombin fragment 1. Seshadri, T.P., Skrzypczak-Jankun, E., Yin, M. et al. Biochemistry (1994) 33:1087-1092. DOI 10.1021/bi00171a006 · PubMed
Other PDB entries of the same protein (UniProt P00735 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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