Crystallographic analysis of counter-ion effects on subtilisin enzymatic action in acetonitrile. Determined by X-ray diffraction at 2.24 Å resolution. Released 8 Dec 2010.
Explore 2WUV in 3D Show helices and sheets RCSB PDB PDBe
2WUV contains 11 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 | 13-17 | 5 | |
| 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 | 196-201 | 6 | 1 |
| β-strand | 205-209 | 5 | 4 |
| β-strand | 213-217 | 5 | 4 |
| α-helix | 220-237 | 18 | |
| α-helix | 243-252 | 10 | |
| β-strand | 255 | 1 | 1 |
| α-helix | 260-263 | 4 | |
| β-strand | 267 | 1 | 1 |
| α-helix | 270-274 | 5 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Subtilisin carlsberg | A | protein | 274 | BACILLUS LICHENIFORMIS | P00780 (AlphaFold model) |
>2WUV_1 SUBTILISIN CARLSBERG (chains A) AQTVPYGIPLIKADKVQAQGFKGANVKVAVLDTGIQASHPDLNVVGGASFVAGEAYNTDG NGHGTHVAGTVAALDNTTGVLGVAPSVSLYAVKVLNSSGSGSYSGIVSGIEWATTNGMDV INMSLGGASGSTAMKQAVDNAYARGVVVVAAAGNSGNSGSTNTIGYPAKYDSVIAVGAVD SNSNRASFSSVGAELEVMAPGAGVYSTYPTNTYATLNGTSMASPHVAGAAALILSKHPNL SASQVRNRLSSTATYLGSSFYYGKGLINVEAAAQ
Water and common crystallization additives (NA, CL) are not listed.
Crystallographic Analysis of Counterion Effects on Subtilisin Enzymatic Action in Acetonitrile. Cianci, M., Tomaszewski, B., Helliwell, J.R. et al. J Am Chem Soc (2010) 132:2293. DOI 10.1021/JA908703C · 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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