Crystal Structure of the Recombinant Human Alpha I Tryptase Mutant D216G. Determined by X-ray diffraction at 2.1 Å resolution. Released 31 Jan 2006.
Explore 2F9O in 3D Show helices and sheets RCSB PDB PDBe
2F9O contains 40 α-helices and 104 β-strands across 4 chains. 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 |
|---|---|---|---|
| β-strand | 17 | 1 | 1 |
| β-strand | 20-21 | 2 | 2 |
| α-helix | 22-23 | 2 | |
| β-strand | 30-36 | 7 | 3 |
| β-strand | 38-48 | 11 | 3 |
| β-strand | 51-54 | 4 | 3 |
| α-helix | 56-58 | 3 | |
| β-strand | 60B | 1 | 4 |
| α-helix | 61-63 | 3 | |
| β-strand | 64-67 | 4 | 3 |
| β-strand | 72 | 1 | 5 |
| β-strand | 83 | 1 | 3 |
| β-strand | 85-90 | 6 | 3 |
| α-helix | 97-99 | 3 | |
| β-strand | 104-108 | 5 | 3 |
| α-helix | 111-114 | 4 | |
| β-strand | 122 | 1 | 2 |
| α-helix | 123-125 | 3 | |
| β-strand | 136-140 | 5 | 2 |
| β-strand | 145 | 1 | 6 |
| β-strand | 149 | 1 | 6 |
| α-helix | 150-152 | 3 | |
| β-strand | 154 | 1 | 5 |
| β-strand | 156-159 | 4 | 2 |
| β-strand | 162-163 | 2 | 2 |
| α-helix | 165-173 | 9 | |
| β-strand | 173C | 1 | 7 |
| β-strand | 180-183 | 4 | 2 |
| β-strand | 189 | 1 | 1 |
| β-strand | 198-203 | 6 | 2 |
| β-strand | 206-215 | 10 | 2 |
| β-strand | 221A | 1 | 8 |
| β-strand | 224 | 1 | 8 |
| β-strand | 226-230 | 5 | 2 |
| α-helix | 231-234 | 4 | |
| α-helix | 235-238 | 4 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 17 | 1 | 9 |
| β-strand | 20-21 | 2 | 10 |
| α-helix | 22-23 | 2 | |
| β-strand | 30-37 | 8 | 11 |
| β-strand | 37B-48 | 12 | 11 |
| β-strand | 51-54 | 4 | 11 |
| α-helix | 56-58 | 3 | |
| β-strand | 60B | 1 | 12 |
| α-helix | 61-63 | 3 | |
| β-strand | 64-67 | 4 | 11 |
| β-strand | 72 | 1 | 13 |
| β-strand | 83 | 1 | 11 |
| β-strand | 85-90 | 6 | 11 |
| α-helix | 97-99 | 3 | |
| β-strand | 104-108 | 5 | 11 |
| α-helix | 111-114 | 4 | |
| β-strand | 122 | 1 | 10 |
| α-helix | 123-125 | 3 | |
| β-strand | 136-140 | 5 | 10 |
| β-strand | 145 | 1 | 14 |
| β-strand | 149 | 1 | 14 |
| α-helix | 150-152 | 3 | |
| β-strand | 154 | 1 | 13 |
| β-strand | 156-159 | 4 | 10 |
| β-strand | 162-163 | 2 | 10 |
| α-helix | 165-173 | 9 | |
| β-strand | 173C | 1 | 15 |
| β-strand | 180-183 | 4 | 10 |
| β-strand | 189 | 1 | 9 |
| β-strand | 198-203 | 6 | 10 |
| β-strand | 206-215 | 10 | 10 |
| β-strand | 221A | 1 | 16 |
| β-strand | 224 | 1 | 16 |
| β-strand | 226-230 | 5 | 10 |
| α-helix | 231-234 | 4 | |
| α-helix | 235-241 | 7 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 17 | 1 | 23 |
| β-strand | 20-21 | 2 | 24 |
| α-helix | 22-23 | 2 | |
| β-strand | 30-37 | 8 | 25 |
| β-strand | 37B-48 | 12 | 25 |
| β-strand | 51-54 | 4 | 25 |
| α-helix | 56-58 | 3 | |
| β-strand | 60B | 1 | 7 |
| α-helix | 61-63 | 3 | |
| β-strand | 64-67 | 4 | 25 |
| β-strand | 72 | 1 | 26 |
| β-strand | 83 | 1 | 25 |
| β-strand | 85-90 | 6 | 25 |
| α-helix | 97-99 | 3 | |
| β-strand | 104-108 | 5 | 25 |
| α-helix | 111-114 | 4 | |
| β-strand | 122 | 1 | 24 |
| α-helix | 123-125 | 3 | |
| β-strand | 136-140 | 5 | 24 |
| β-strand | 145 | 1 | 27 |
| β-strand | 149 | 1 | 27 |
| α-helix | 150-152 | 3 | |
| β-strand | 154 | 1 | 26 |
| β-strand | 156-159 | 4 | 24 |
| β-strand | 162-163 | 2 | 24 |
| α-helix | 165-173 | 9 | |
| β-strand | 173C | 1 | 4 |
| β-strand | 180-183 | 4 | 24 |
| β-strand | 189 | 1 | 23 |
| β-strand | 198-203 | 6 | 24 |
| β-strand | 206-215 | 10 | 24 |
| β-strand | 221A | 1 | 28 |
| β-strand | 224 | 1 | 28 |
| β-strand | 226-230 | 5 | 24 |
| α-helix | 231-234 | 4 | |
| α-helix | 235-239 | 5 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Tryptase alpha-1 | A, B, C, D | protein | 245 | Homo sapiens | Q15661 (AlphaFold model) |
>2F9O_1 Tryptase alpha-1 (chains A, B, C, D) IVGGQEAPRSKWPWQVSLRVRDRYWMHFCGGSLIHPQWVLTAAHCVGPDVKDLATLRVQL REQHLYYQDQLLPVSRIIVHPQFYIIQTGADIALLELEEPVNISSRVHTVMLPPASETFP PGMPCWVTGWGDVDNDEPLPPPFPLKQVKVPIMENHICDAKYHLGAYTGDDVRIIRDDML CAGNSQRDSCKGDSGGPLVCKVNGTWLQAGVVSWGEGCAQPNRPGIYTRVTYYLDWIHHY VPKKP
X-ray Structures of Free and Leupeptin-complexed Human alpha I-Tryptase Mutants: Indication for an alpha to beta-Tryptase Transition. Rohr, K.B., Selwood, T., Marquardt, U. et al. J Mol Biol (2005) 357:195-209. DOI 10.1016/j.jmb.2005.12.037 · PubMed
Other PDB entries of the same protein (UniProt Q15661 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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