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TitleStructural basis for an exceptionally strong preference for asparagine residue at the S2 subsite of Stenotrophomonas maltophilia dipeptidyl peptidase 7.
Journal, issue, pagesSci Rep, Vol. 11, Page 7929-7929, Year 2021
Publish dateNov 23, 2020 (structure data deposition date)
AuthorsNakamura, A. / Suzuki, Y. / Sakamoto, Y. / Roppongi, S. / Kushibiki, C. / Yonezawa, N. / Takahashi, M. / Shida, Y. / Gouda, H. / Nonaka, T. ...Nakamura, A. / Suzuki, Y. / Sakamoto, Y. / Roppongi, S. / Kushibiki, C. / Yonezawa, N. / Takahashi, M. / Shida, Y. / Gouda, H. / Nonaka, T. / Tanaka, N. / Ogasawara, W.
External linksSci Rep / PubMed:33846449
MethodsX-ray diffraction
Resolution1.86 - 2.03 Å
Structure data

PDB-7dkb:
Stenotrophomonas maltophilia DPP7 in complex with Val-Tyr
Method: X-RAY DIFFRACTION / Resolution: 2.03 Å

PDB-7dkc:
Stenotrophomonas maltophilia DPP7 in complex with Tyr-Tyr
Method: X-RAY DIFFRACTION / Resolution: 1.86 Å

PDB-7dkd:
Stenotrophomonas maltophilia DPP7 in complex with Asn-Tyr
Method: X-RAY DIFFRACTION / Resolution: 1.92 Å

PDB-7dke:
Stenotrophomonas maltophilia DPP7 in complex with Phe-Tyr
Method: X-RAY DIFFRACTION / Resolution: 1.91 Å

Chemicals

ChemComp-VAL:
VALINE

ChemComp-TYR:
TYROSINE

ChemComp-HOH:
WATER

ChemComp-GOL:
GLYCEROL

ChemComp-ASN:
ASPARAGINE

ChemComp-PHE:
PHENYLALANINE

Source
  • stenotrophomonas maltophilia (strain r551-3) (bacteria)
KeywordsHYDROLASE / dipeptidyl aminopeptidase / S46 / AMR / Microgravity / antimicrobial / chymotrypsin / serine protease

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