1ADD
A PRE-TRANSITION STATE MIMIC OF AN ENZYME: X-RAY STRUCTURE OF ADENOSINE DEAMINASE WITH BOUND 1-DEAZA-ADENOSINE AND ZINC-ACTIVATED WATER
Summary for 1ADD
| Entry DOI | 10.2210/pdb1add/pdb |
| Descriptor | ADENOSINE DEAMINASE, ZINC ION, 1-DEAZA-ADENOSINE, ... (4 entities in total) |
| Functional Keywords | hydrolase(acting in cyclicamidines) |
| Biological source | Mus musculus (house mouse) |
| Cellular location | Cell membrane; Peripheral membrane protein; Extracellular side (By similarity): P03958 |
| Total number of polymer chains | 1 |
| Total formula weight | 40046.85 |
| Authors | Wilson, D.K.,Quiocho, F.A. (deposition date: 1992-12-22, release date: 1994-01-31, Last modification date: 2024-02-07) |
| Primary citation | Wilson, D.K.,Quiocho, F.A. A pre-transition-state mimic of an enzyme: X-ray structure of adenosine deaminase with bound 1-deazaadenosine and zinc-activated water. Biochemistry, 32:1689-1694, 1993 Cited by PubMed Abstract: The refined 2.4-A structure of adenosine deaminase, recently discovered to be a zinc metalloenzyme [Wilson, D. K., Rudolph, F. B., & Quiocho, F. A. (1991) Science 252, 1278-1284], complexed with the ground-state analog 1-deazaadenosine shows the mode of binding of the analog and, unexpectedly, a zinc-activated water (hydroxide). This structure of a pre-transition-state mimic, combined with that previously determined for the complex with 6(R)-hydroxy-1,6-dihydropurine ribonucleoside, a nearly ideal transition-state analog, sheds new understanding of the precise stereospecificity and hydrolytic catalysis of an important and well-characterized member of a large group of zinc metalloenzymes. As both of these excellent mimics were generated in the active site, they demonstrate a powerful means of dissecting the course of an enzymatic reaction by direct crystallographic analysis. PubMed: 8439534DOI: 10.1021/bi00058a001 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.4 Å) |
Structure validation
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