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-Structure paper
Title | How metal cofactors drive dimer-dodecamer transition of the M42 aminopeptidase TmPep1050 ofThermotoga maritima. |
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Journal, issue, pages | J. Biol. Chem., Vol. 294, Page 17777-17789, Year 2019 |
Publish date | Mar 10, 2017 (structure data deposition date) |
![]() | Dutoit, R. / Van Gompel, T. / Brandt, N. / Van Elder, D. / Van Dyck, J. / Sobott, F. / Droogmans, L. |
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Methods | X-ray diffraction |
Resolution | 1.7 - 2 Å |
Structure data | ![]() PDB-5ne6: ![]() PDB-5ne7: ![]() PDB-5ne8: ![]() PDB-6nw5: |
Chemicals | ![]() ChemComp-CIT: ![]() ChemComp-HOH: ![]() ChemComp-ZN: ![]() ChemComp-CO: ![]() ChemComp-SO4: ![]() ChemComp-OH: |
Source |
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![]() | LYASE / Aminopeptidase / Peptidase M42 / tetrahedral structure / metal ion binding / M42 family / HYDROLASE / M42 aminopeptidase / TET-aminopeptidase / MH clan |