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-Structure paper
Title | Structural basis for an exceptionally strong preference for asparagine residue at the S2 subsite of Stenotrophomonas maltophilia dipeptidyl peptidase 7. |
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Journal, issue, pages | Sci Rep, Vol. 11, Page 7929-7929, Year 2021 |
Publish date | Nov 23, 2020 (structure data deposition date) |
![]() | Nakamura, 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. |
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Methods | X-ray diffraction |
Resolution | 1.86 - 2.03 Å |
Structure data | ![]() PDB-7dkb: ![]() PDB-7dkc: ![]() PDB-7dkd: ![]() PDB-7dke: |
Chemicals | ![]() ChemComp-VAL: ![]() ChemComp-TYR: ![]() ChemComp-HOH: ![]() ChemComp-GOL: ![]() ChemComp-ASN: ![]() ChemComp-PHE: |
Source |
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![]() | HYDROLASE / dipeptidyl aminopeptidase / S46 / AMR / Microgravity / antimicrobial / chymotrypsin / serine protease |