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-Structure paper
Title | Structural and kinetic bases for the metal preference of the M18 aminopeptidase from Pseudomonas aeruginosa |
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Journal, issue, pages | Biochem. Biophys. Res. Commun., Vol. 447, Page 101-107, Year 2014 |
Publish date | Apr 7, 2014 (structure data deposition date) |
Authors | Nguyen, D.D. / Pandian, R. / Kim, D. / Ha, S.C. / Yoon, H.J. / Kim, K.S. / Yun, K.H. / Kim, J.H. / Kim, K.K. |
External links | Biochem. Biophys. Res. Commun. / PubMed:24704201 |
Methods | X-ray diffraction |
Resolution | 2.3 - 2.702 Å |
Structure data | PDB-3wt4: PDB-4njq: PDB-4njr: PDB-4oid: PDB-4oiw: |
Chemicals | ChemComp-ZN: ChemComp-CO3: ChemComp-HOH: ChemComp-CO: ChemComp-NHE: |
Source |
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Keywords | HYDROLASE / aspartyl aminopeptidase / TET shape protease / dodecameric peptidase / dodecameric tetraheral shape / metallopeptidase / cobalt complex / Tetrahedral shape dodecameric structure / Metal binding / Dodecameric TET structure / Pseudomonas aeruginosa / Aspartic mutation / M18 family / Histidine mutation |