Human mesotrypsin complexed with HAI-2 Kunitz domain 1. Determined by X-ray diffraction at 1.65 Å resolution. Released 15 Oct 2014.
Explore 4U32 in 3D Show helices and sheets RCSB PDB PDBe
4U32 contains 9 α-helices and 24 β-strands across 2 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 | 3 |
| β-strand | 20-21 | 2 | 1 |
| α-helix | 22-23 | 2 | |
| β-strand | 30-34 | 5 | 4 |
| β-strand | 40-46 | 7 | 4 |
| β-strand | 51-54 | 4 | 4 |
| α-helix | 56-58 | 3 | |
| β-strand | 64-67 | 4 | 4 |
| β-strand | 72 | 1 | 5 |
| β-strand | 81-90 | 10 | 4 |
| β-strand | 104-108 | 5 | 4 |
| α-helix | 111-114 | 4 | |
| β-strand | 115 | 1 | 6 |
| β-strand | 118 | 1 | 6 |
| β-strand | 122 | 1 | 1 |
| α-helix | 123-124 | 2 | |
| β-strand | 135-140 | 6 | 1 |
| β-strand | 154 | 1 | 5 |
| β-strand | 156-162 | 7 | 1 |
| α-helix | 163-164 | 2 | |
| α-helix | 165-171 | 7 | |
| β-strand | 180-183 | 4 | 1 |
| β-strand | 189 | 1 | 3 |
| β-strand | 198-201 | 4 | 1 |
| β-strand | 204-215 | 8 | 1 |
| β-strand | 226-230 | 5 | 1 |
| α-helix | 231-234 | 4 | |
| α-helix | 235-244 | 10 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 14 | 1 | 1 |
| β-strand | 18-24 | 7 | 2 |
| β-strand | 29-35 | 7 | 2 |
| β-strand | 45 | 1 | 2 |
| α-helix | 48-54 | 7 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Kunitz-type protease inhibitor 2 | X | protein | 55 | Homo sapiens | O43291 (AlphaFold model) |
| Trypsin-3 | A | protein | 224 | Homo sapiens | P35030 (AlphaFold model) |
>4U32_1 Kunitz-type protease inhibitor 2 (chains X) IHDFCLVSKVVGRCRASMPRWWYNVTDGSCQLFVYGGCDGNSNNYLTKEECLKKC
>4U32_2 Trypsin-3 (chains A) IVGGYTCEENSLPYQVSLNSGSHFCGGSLISEQWVVSAAHCYKTRIQVRLGEHNIKVLEG NEQFINAAKIIRHPKYNRDTLDNDIMLIKLSSPAVINARVSTISLPTAPPAAGTECLISG WGNTLSFGADYPDELKCLDAPVLTQAECKASYPGKITNSMFCVGFLEGGKDSCQRDAGGP VVCNGQLQGVVSWGHGCAWKNRPGVYTKVYNYVDWIKDTIAANS
Sequence and Conformational Specificity in Substrate Recognition: SEVERAL HUMAN KUNITZ PROTEASE INHIBITOR DOMAINS ARE SPECIFIC SUBSTRATES OF MESOTRYPSIN. Pendlebury, D., Wang, R., Henin, R.D. et al. J Biol Chem (2014) 289:32783-32797. DOI 10.1074/jbc.M114.609560 · PubMed
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