Crystal structure of selenosubtilisin at 2.0-Å resolution. Determined by X-ray diffraction at 2.0 Å resolution. Released 31 Oct 1993.
Explore 1SEL in 3D Show helices and sheets RCSB PDB PDBe
1SEL contains 25 α-helices and 32 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 | 7-10 | 4 | |
| α-helix | 13-19 | 7 | |
| β-strand | 27-32 | 6 | 1 |
| β-strand | 44-49 | 6 | 1 |
| α-helix | 64-73 | 10 | |
| β-strand | 89-94 | 6 | 1 |
| α-helix | 104-116 | 13 | |
| β-strand | 121-124 | 4 | 1 |
| β-strand | 128 | 1 | 2 |
| α-helix | 133-144 | 12 | |
| β-strand | 148-152 | 5 | 1 |
| β-strand | 159 | 1 | 3 |
| β-strand | 162 | 1 | 3 |
| β-strand | 167 | 1 | 2 |
| β-strand | 175-180 | 6 | 1 |
| α-helix | 185 | 1 | |
| β-strand | 186 | 1 | 1 |
| α-helix | 187 | 1 | |
| β-strand | 198-201 | 4 | 1 |
| β-strand | 205-209 | 5 | 4 |
| β-strand | 213-217 | 5 | 4 |
| α-helix | 220-237 | 18 | |
| α-helix | 243-252 | 10 | |
| α-helix | 254 | 1 | |
| β-strand | 255 | 1 | 1 |
| α-helix | 256 | 1 | |
| α-helix | 260-263 | 4 | |
| β-strand | 267 | 1 | 1 |
| α-helix | 270-273 | 4 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 7-10 | 4 | |
| α-helix | 13-18 | 6 | |
| β-strand | 27-32 | 6 | 5 |
| β-strand | 44-49 | 6 | 5 |
| α-helix | 64-73 | 10 | |
| α-helix | 74-76 | 3 | |
| β-strand | 89-94 | 6 | 5 |
| α-helix | 104-116 | 13 | |
| β-strand | 121-124 | 4 | 5 |
| β-strand | 128 | 1 | 6 |
| α-helix | 133-144 | 12 | |
| β-strand | 148-152 | 5 | 5 |
| β-strand | 159 | 1 | 7 |
| β-strand | 161-162 | 2 | 7 |
| β-strand | 167 | 1 | 6 |
| β-strand | 175-180 | 6 | 5 |
| β-strand | 186 | 1 | 5 |
| β-strand | 198-201 | 4 | 5 |
| β-strand | 205-209 | 5 | 8 |
| β-strand | 213-217 | 5 | 8 |
| α-helix | 220-237 | 18 | |
| α-helix | 243-252 | 10 | |
| α-helix | 254 | 1 | |
| β-strand | 255 | 1 | 5 |
| α-helix | 256 | 1 | |
| α-helix | 260-263 | 4 | |
| β-strand | 267 | 1 | 5 |
| α-helix | 270-273 | 4 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Selenosubtilisin | A, B | protein | 274 | Bacillus subtilis | P00780 (AlphaFold model) |
>1SEL_1 SELENOSUBTILISIN (chains A, B) AQTVPYGIPLIKADKVQAQGFKGANVKVAVLDTGIQASHPDLNVVGGASFVAGEAYNTDG NGHGTHVAGTVAALDNTTGVLGVAPSVSLYAVKVLNSSGSGSYSGIVSGIEWATTNGMDV INMSLGGASGSTAMKQAVDNAYARGVVVVAAAGNSGNSGSTNTIGYPAKYDSVIAVGAVD SNSNRASFSSVGAELEVMAPGAGVYSTYPTNTYATLNGTUMASPHVAGAAALILSKHPNL SASQVRNRLSSTATYLGSSFYYGKGLINVEAAAQ
| ID | Name | Formula | Copies |
|---|---|---|---|
| CA | Calcium ion | Ca | 4 |
Crystal structure of selenosubtilisin at 2.0-A resolution. Syed, R., Wu, Z.P., Hogle, J.M. et al. Biochemistry (1993) 32:6157-6164. DOI 10.1021/bi00075a007 · PubMed
Other PDB entries of the same protein (UniProt P00780 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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