Subtilisin carlsberg D-para-chlorophenyl-1-acetamido boronic acid inhibitor complex. Determined by X-ray diffraction at 2.0 Å resolution. Released 25 Mar 1998.
Explore 1AVT in 3D Show helices and sheets RCSB PDB PDBe
1AVT contains 13 α-helices and 16 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 |
|---|---|---|---|
| α-helix | 7-10 | 4 | |
| α-helix | 13-18 | 6 | |
| 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 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Subtilisin carlsberg, type VIII | A | protein | 274 | Bacillus licheniformis | P00780 (AlphaFold model) |
>1AVT_1 SUBTILISIN CARLSBERG, TYPE VIII (chains A) AQTVPYGIPLIKADKVQAQGFKGANVKVAVLDTGIQASHPDLNVVGGASFVAGEAYNTDG NGHGTHVAGTVAALDNTTGVLGVAPSVSLYAVKVLNSSGSGSYSGIVSGIEWATTNGMDV INMSLGGASGSTAMKQAVDNAYARGVVVVAAAGNSGNSGSTNTIGYPAKYDSVIAVGAVD SNSNRASFSSVGAELEVMAPGAGVYSTYPTNTYATLNGTXMASPHVAGAAALILSKHPNL SASQVRNRLSSTATYLGSSFYYGKGLINVEAAAQ
Differences in binding modes of enantiomers of 1-acetamido boronic acid based protease inhibitors: crystal structures of gamma-chymotrypsin and subtilisin Carlsberg complexes. Stoll, V.S., Eger, B.T., Hynes, R.C. et al. Biochemistry (1998) 37:451-462. DOI 10.1021/bi971166o · 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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