2WUW: Subtilisin carlsberg

Crystallographic analysis of counter-ion effects on subtilisin enzymatic action in acetonitrile (native data). Determined by X-ray diffraction at 2.23 Å resolution. Released 8 Dec 2010.

Method
X-ray diffraction
Resolution
2.23 Å
Organism
BACILLUS LICHENIFORMIS
Chains
1
Atoms
2,068
Mol. weight
27.69 kDa
Ligands
CA, CCN
Released
8 Dec 2010

Explore 2WUW in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2WUW contains 11 α-helices and 14 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.

Chain E: 11 helices, 14 β-strands

ElementResiduesLengthSheet
α-helix7-104
α-helix13-186
β-strand27-3261
β-strand44-4961
α-helix64-7310
β-strand89-9461
α-helix104-11613
β-strand121-12441
β-strand12812
α-helix133-14412
β-strand148-15251
β-strand16712
β-strand175-18061
α-helix1851
β-strand18611
α-helix1871
β-strand196-20161
β-strand205-20953
β-strand213-21753
α-helix220-23718
α-helix243-25210
β-strand25511
α-helix260-2634
β-strand26711
α-helix270-2734

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Subtilisin carlsbergEprotein274BACILLUS LICHENIFORMISP00780 (AlphaFold model)
Sequence of entity 1 (E), FASTA
>2WUW_1 SUBTILISIN CARLSBERG (chains E)
AQTVPYGIPLIKADKVQAQGFKGANVKVAVLDTGIQASHPDLNVVGGASFVAGEAYNTDG
NGHGTHVAGTVAALDNTTGVLGVAPSVSLYAVKVLNSSGSGSYSGIVSGIEWATTNGMDV
INMSLGGASGSTAMKQAVDNAYARGVVVVAAAGNSGNSGSTNTIGYPAKYDSVIAVGAVD
SNSNRASFSSVGAELEVMAPGAGVYSTYPTNTYATLNGTSMASPHVAGAAALILSKHPNL
SASQVRNRLSSTATYLGSSFYYGKGLINVEAAAQ

Ligands and cofactors

IDNameFormulaCopies
CACalcium ionCa1
CCNAcetonitrileC2 H3 N5

Water and common crystallization additives (SO4, NA) are not listed.

Primary citation

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:

Browse structure collections

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