Structure of Porcine Trypsin Crystals Grown From PEG and Complexed With Crystallization Additives IV. Determined by X-ray diffraction at 1.18 Å resolution. Released 24 Sept 2025.
Explore 9PDA in 3D Show helices and sheets RCSB PDB PDBe
9PDA contains 36 α-helices and 76 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 | 30-34 | 5 | 3 |
| β-strand | 38-46 | 9 | 3 |
| β-strand | 49-52 | 4 | 3 |
| α-helix | 54-56 | 3 | |
| β-strand | 62-65 | 4 | 3 |
| β-strand | 69 | 1 | 4 |
| β-strand | 78-87 | 10 | 3 |
| β-strand | 101-105 | 5 | 3 |
| α-helix | 108-111 | 4 | |
| β-strand | 119 | 1 | 2 |
| α-helix | 120-121 | 2 | |
| α-helix | 124-126 | 3 | |
| β-strand | 130-135 | 6 | 2 |
| β-strand | 149 | 1 | 4 |
| β-strand | 151-157 | 7 | 2 |
| α-helix | 158-159 | 2 | |
| α-helix | 160-166 | 7 | |
| β-strand | 175-178 | 4 | 2 |
| β-strand | 186 | 1 | 1 |
| β-strand | 195-198 | 4 | 2 |
| β-strand | 201-208 | 8 | 2 |
| β-strand | 219-223 | 5 | 2 |
| α-helix | 224-227 | 4 | |
| α-helix | 228-236 | 9 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 17 | 1 | 5 |
| β-strand | 20-21 | 2 | 6 |
| α-helix | 22-23 | 2 | |
| β-strand | 30-34 | 5 | 7 |
| β-strand | 38-46 | 9 | 7 |
| β-strand | 49-52 | 4 | 7 |
| α-helix | 54-56 | 3 | |
| β-strand | 62-65 | 4 | 7 |
| β-strand | 69 | 1 | 8 |
| β-strand | 78-87 | 10 | 7 |
| β-strand | 101-105 | 5 | 7 |
| α-helix | 108-111 | 4 | |
| β-strand | 112 | 1 | 9 |
| β-strand | 115 | 1 | 9 |
| β-strand | 119 | 1 | 6 |
| α-helix | 120-121 | 2 | |
| α-helix | 124-126 | 3 | |
| β-strand | 130-135 | 6 | 6 |
| β-strand | 149 | 1 | 8 |
| α-helix | 150 | 1 | |
| β-strand | 151-157 | 7 | 6 |
| α-helix | 158-159 | 2 | |
| α-helix | 160-166 | 7 | |
| β-strand | 175-178 | 4 | 6 |
| β-strand | 186 | 1 | 5 |
| β-strand | 195-198 | 4 | 6 |
| β-strand | 201-208 | 8 | 6 |
| β-strand | 214 | 1 | 10 |
| β-strand | 217 | 1 | 10 |
| β-strand | 219-223 | 5 | 6 |
| α-helix | 224-226 | 3 | |
| α-helix | 228-237 | 10 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 17 | 1 | 15 |
| β-strand | 20-21 | 2 | 16 |
| α-helix | 22-23 | 2 | |
| β-strand | 30-34 | 5 | 17 |
| β-strand | 38-46 | 9 | 17 |
| β-strand | 49-52 | 4 | 17 |
| α-helix | 54-56 | 3 | |
| β-strand | 62-65 | 4 | 17 |
| β-strand | 69 | 1 | 18 |
| β-strand | 78-87 | 10 | 17 |
| β-strand | 101-105 | 5 | 17 |
| β-strand | 119 | 1 | 16 |
| α-helix | 120-121 | 2 | |
| α-helix | 124-126 | 3 | |
| β-strand | 130-135 | 6 | 16 |
| β-strand | 149 | 1 | 18 |
| β-strand | 151-157 | 7 | 16 |
| α-helix | 158-159 | 2 | |
| α-helix | 160-166 | 7 | |
| β-strand | 175-178 | 4 | 16 |
| β-strand | 186 | 1 | 15 |
| β-strand | 195-198 | 4 | 16 |
| β-strand | 201-208 | 8 | 16 |
| β-strand | 219-223 | 5 | 16 |
| α-helix | 224-226 | 3 | |
| α-helix | 228-237 | 10 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Trypsin | A, B, C, D | protein | 231 | Sus scrofa | P00761 (AlphaFold model) |
>9PDA_1 Trypsin (chains A, B, C, D) FPTDDDDKIVGGYTCAANSIPYQVSLNSGSHFCGGSLINSQWVVSAAHCYKSRIQVRLGE HNIDVLEGNEQFINAAKIITHPNFNGNTLDNDIMLIKLSSPATLNSRVATVSLPRSCAAA GTECLISGWGNTKSSGSSYPSLLQCLKAPVLSDSSCKSSYPGQITGNMICVGFLEGGKDS CQGDSGGPVVCNGQLQGIVSWGYGCAQKNKPGVYTKVCNYVNWIQQTIAAN
| ID | Name | Formula | Copies |
|---|---|---|---|
| BEN | Benzamidine | C7 H8 N2 | 10 |
| PG5 | 1-methoxy-2-[2-(2-methoxy-ethoxy]-ethane | C8 H18 O4 | 12 |
| PG6 | 1-(2-methoxy-ethoxy)-2-{2-[2-(2-methoxy-ethoxy]-ethoxy}-ethane | C12 H26 O6 | 1 |
| CA | Calcium ion | Ca | 5 |
| MLI | Malonate ion | C3 H2 O4 | 4 |
| PMA | Pyromellitic acid | C10 H6 O8 | 2 |
Water and common crystallization additives (PEG, PG4, EPE, CL) are not listed.
X-ray Diffraction Analyses of Trypsin Crystals Grown in the Presence of Additives. McPherson, A. Cryst Growth Des (2026) 26:352-364. DOI 10.1021/acs.cgd.5c01305
Other PDB entries of the same protein (UniProt P00761 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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