Bovine trypsin at 0.8 A resolution, non-restrained refinement. Determined by X-ray diffraction at 0.8 Å resolution. Released 28 Apr 2010.
Explore 3MI4 in 3D Show helices and sheets RCSB PDB PDBe
3MI4 contains 6 α-helices and 20 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 |
|---|---|---|---|
| β-strand | 17 | 1 | 1 |
| β-strand | 20-21 | 2 | 2 |
| β-strand | 30-34 | 5 | 3 |
| β-strand | 40-48 | 9 | 3 |
| β-strand | 51-54 | 4 | 3 |
| α-helix | 56-58 | 3 | |
| β-strand | 64-67 | 4 | 3 |
| β-strand | 81-90 | 10 | 3 |
| β-strand | 104-108 | 5 | 3 |
| β-strand | 115 | 1 | 4 |
| β-strand | 118 | 1 | 4 |
| β-strand | 122 | 1 | 2 |
| α-helix | 123-124 | 2 | |
| β-strand | 135-140 | 6 | 2 |
| β-strand | 156-162 | 7 | 2 |
| α-helix | 163-164 | 2 | |
| α-helix | 165-171 | 7 | |
| β-strand | 180-183 | 4 | 2 |
| β-strand | 189 | 1 | 1 |
| β-strand | 198-201 | 4 | 2 |
| β-strand | 204-215 | 8 | 2 |
| β-strand | 221A | 1 | 5 |
| β-strand | 224 | 1 | 5 |
| β-strand | 226-230 | 5 | 2 |
| α-helix | 231-234 | 4 | |
| α-helix | 235-244 | 10 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Cationic trypsin | A | protein | 223 | Bos taurus | P00760 (AlphaFold model) |
>3MI4_1 Cationic trypsin (chains A) IVGGYTCGANTVPYQVSLNSGYHFCGGSLINSQWVVSAAHCYKSGIQVRLGEDNINVVEG NEQFISASKSIVHPSYNSNTLNNDIMLIKLKSAASLNSRVASISLPTSCASAGTQCLISG WGNTKSSGTSYPDVLKCLKAPILSDSSCKSAYPGQITSNMFCAGYLEGGKDSCQGDSGGP VVCSGKLQGIVSWGSGCAQKNKPGVYTKVCNYVSWIKQTIASN
Water and common crystallization additives (GOL, SO4) are not listed.
Bovine trypsin at 0.8 A and role of restraints at ultra-high resolution. Brzuszkiewicz, A., Dauter, M., Dauter, Z. To be published.
Other PDB entries of the same protein (UniProt P00760 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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