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-Structure paper
Title | Removal of the Side Chain at the Active-Site Serine by a Glycine Substitution Increases the Stability of a Wide Range of Serine beta-Lactamases by Relieving Steric Strain. |
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Journal, issue, pages | Biochemistry, Vol. 55, Page 2479-2490, Year 2016 |
Publish date | Dec 30, 2015 (structure data deposition date) |
Authors | Stojanoski, V. / Adamski, C.J. / Hu, L. / Mehta, S.C. / Sankaran, B. / Zwart, P. / Prasad, B.V. / Palzkill, T. |
External links | Biochemistry / PubMed:27073009 |
Methods | X-ray diffraction |
Resolution | 1.74 - 2.74 Å |
Structure data | PDB-5hai: PDB-5hap: PDB-5haq: PDB-5har: |
Chemicals | ChemComp-PO4: ChemComp-HOH: ChemComp-CL: ChemComp-1PE: ChemComp-PGE: ChemComp-NA: ChemComp-PEG: ChemComp-MPD: ChemComp-PG4: ChemComp-EDO: ChemComp-CD: ChemComp-FMT: ChemComp-ACT: |
Source |
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Keywords | HYDROLASE / serine beta-lactamase |