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Structure paper

TitleSubstrate specificity in a designed RAS-targeting protease is coupled to active site and distal motions.
Journal, issue, pagesBiorxiv, Year 2026
Publish dateDec 4, 2025 (structure data deposition date)
AuthorsChu, B. / He, Y. / Chen, Y. / Toth, E.A. / Orban, J.
External linksBiorxiv / PubMed:41648245
MethodsX-ray diffraction
Resolution1.2 - 1.49 Å
Structure data

PDB-9zio:
Crystal Structure of RASProtease(II), a Designed RAS-specific Subtilisin
Method: X-RAY DIFFRACTION / Resolution: 1.49 Å

PDB-9zip:
Crystal Structure of RASProtease(II), a Designed RAS-specific Subtilisin, in Complex with the Cognate Peptide QEEYSAM
Method: X-RAY DIFFRACTION / Resolution: 1.24 Å

PDB-9ziq:
Crystal Structure of RASProtease(II), a Designed RAS-specific Subtilisin, in Complex with the Non-cognate Peptide QEEISAM
Method: X-RAY DIFFRACTION / Resolution: 1.2 Å

Chemicals

ChemComp-EDO:
1,2-ETHANEDIOL

ChemComp-GOL:
GLYCEROL

ChemComp-NA:
Unknown entry

ChemComp-PEG:
DI(HYDROXYETHYL)ETHER

ChemComp-FMT:
FORMIC ACID

ChemComp-HOH:
WATER

ChemComp-K:
Unknown entry

ChemComp-ACT:
ACETATE ION

ChemComp-ZN:
Unknown entry

ChemComp-DMS:
DIMETHYL SULFOXIDE / DMSO, precipitant*YM

Source
  • bacillus amyloliquefaciens (bacteria)
  • synthetic construct (others)
KeywordsHYDROLASE / Engineered protease

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