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Literature summary for 2.7.4.3 extracted from
- Structure of the complex between adenylate kinase from Escherichia coli and the inhibitor Ap5A refined at 1.9 A resolution. a model for a catalytic transition state (1992), J. Mol. Biol., 224, 159-177.
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
| in complex with inhibitor P1,P5-di(adenosine-5)-pentaphosphate that simulates well the binding of substrates ATP and AMP. The alpha-phosphate of AMP is well positioned for a nucleophilic attack on the gamma-phosphate of ATP, giving a stabilized pentacoordinated transition state with nucleophile and leaving group in the apical positions of a trigonal bipyramide | Escherichia coli |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| P1,P5-di(adenosine-5')pentaphosphate | - |
Escherichia coli |  |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Escherichia coli | - |
- |
- |
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