7P75
Re-engineered 2-deoxy-D-ribose-5-phosphate aldolase catalysing asymmetric Michael addition reactions in substrate-free state
This is a non-PDB format compatible entry.
Summary for 7P75
Entry DOI | 10.2210/pdb7p75/pdb |
Descriptor | Deoxyribose-phosphate aldolase (2 entities in total) |
Functional Keywords | protein engineering, directed evolution, dera, aldolase, carboligase, michael addition, carbon-carbon lyase, lyase |
Biological source | Escherichia coli (strain ATCC 8739 / DSM 1576 / NBRC 3972 / NCIMB 8545 / WDCM 00012 / Crooks) |
Total number of polymer chains | 2 |
Total formula weight | 57367.48 |
Authors | Thunnissen, A.M.W.H.,Rozeboom, H.J.,Kunzendorf, A.,Poelarends, G.J. (deposition date: 2021-07-19, release date: 2021-10-27, Last modification date: 2024-01-31) |
Primary citation | Kunzendorf, A.,Xu, G.,van der Velde, J.J.H.,Rozeboom, H.J.,Thunnissen, A.W.H.,Poelarends, G.J. Unlocking Asymmetric Michael Additions in an Archetypical Class I Aldolase by Directed Evolution. Acs Catalysis, 11:13236-13243, 2021 Cited by PubMed: 34765282DOI: 10.1021/acscatal.1c03911 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.23 Å) |
Structure validation
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