Rat anionic N143H, E151H trypsin complexed to A86H ecotin; nickel-bound. Determined by X-ray diffraction at 2.0 Å resolution. Released 11 Jul 1996.
Explore 1SLW in 3D Show helices and sheets RCSB PDB PDBe
1SLW contains 16 α-helices and 31 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 |
|---|---|---|---|
| α-helix | 13-17 | 5 | |
| β-strand | 20-25 | 6 | 1 |
| α-helix | 27-29 | 3 | |
| α-helix | 33-35 | 3 | |
| β-strand | 36-48 | 13 | 2 |
| β-strand | 53-54 | 2 | 1 |
| β-strand | 55 | 1 | 3 |
| β-strand | 56-64 | 9 | 1 |
| β-strand | 69-83 | 15 | 1 |
| α-helix | 85-87 | 3 | |
| β-strand | 93-98 | 6 | 2 |
| β-strand | 99 | 1 | 3 |
| β-strand | 106-108 | 3 | 2 |
| α-helix | 109 | 1 | |
| β-strand | 115-120 | 6 | 1 |
| β-strand | 124-131 | 8 | 2 |
| α-helix | 139-141 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 17 | 1 | 4 |
| β-strand | 20-21 | 2 | 1 |
| α-helix | 22-23 | 2 | |
| β-strand | 30-34 | 5 | 5 |
| β-strand | 40-48 | 9 | 5 |
| β-strand | 51-54 | 4 | 5 |
| α-helix | 56-58 | 3 | |
| β-strand | 64-66 | 3 | 5 |
| β-strand | 72 | 1 | 6 |
| β-strand | 82-90 | 9 | 5 |
| β-strand | 95 | 1 | 7 |
| β-strand | 100 | 1 | 7 |
| β-strand | 104-108 | 5 | 5 |
| α-helix | 120-121 | 2 | |
| β-strand | 122 | 1 | 1 |
| α-helix | 123-124 | 2 | |
| α-helix | 128-130 | 3 | |
| β-strand | 135-140 | 6 | 1 |
| β-strand | 154 | 1 | 6 |
| α-helix | 155 | 1 | |
| 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 | 4 |
| β-strand | 198-201 | 4 | 1 |
| β-strand | 204-216 | 9 | 1 |
| β-strand | 226-230 | 5 | 1 |
| α-helix | 231-234 | 4 | |
| α-helix | 235-243 | 9 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Ecotin | A | protein | 142 | Escherichia coli | P23827 (AlphaFold model) |
| Anionic trypsin | B | protein | 223 | Rattus norvegicus | P00763 (AlphaFold model) |
>1SLW_1 ECOTIN (chains A) AESVQPLEKIAPYPQAEKGMKRQVIQLTPQEDESTLKVELLIGQTLEVDCNLHRLGGKLE NKTLEGWGYDYYVFDKVSSPVSTMMHCPDGKKEKKFVTAYLGDAGMLRYNSKLPIVVYTP DNVDVKYRVWKAEEKIDNAVVR
>1SLW_2 ANIONIC TRYPSIN (chains B) IVGGYTCQENSVPYQVSLNSGYHFCGGSLINDQWVVSAAHCYKSRIQVRLGEHNINVLEG NEQFVNAAKIIKHPNFDRKTLNNDIMLIKLSSPVKLNARVATIALPSSCAPAGTQCLISG WGHTLSSGVNHPDLLQCLDAPLLPQADCEASYPGKITDNMVCVGFLEGGKDSCQGDSGGP VVCNGELQGIVSWGYGCALPDNPGVYTKVCNYVDWIQDTIAAN
Water and common crystallization additives (ACT) are not listed.
X-ray structures of a designed binding site in trypsin show metal-dependent geometry. Brinen, L.S., Willett, W.S., Craik, C.S. et al. Biochemistry (1996) 35:5999-6009. DOI 10.1021/bi9530200 · PubMed
Other PDB entries of the same protein (UniProt P23827 (AlphaFold model), which also has an AlphaFold model), best resolution first:
MolViewer shows 1SLW directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.