1a4l
ADA STRUCTURE COMPLEXED WITH DEOXYCOFORMYCIN AT PH 7.0
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OverviewOverview
Adenosine deaminase, which catalyzes the irreversible hydrolytic, deamination of adenosine nucleosides to inosine nucleosides and ammonia, is a key enzyme in purine metabolism and lymphoid development. The X-ray, structures of murine adenosine deaminase with bound potent inhibitors (Ki, values approximately 10(-13) M) (8R)-hydroxyl-2'-deoxycoformycin, (pentostatin), a transition state analogue, and, (6S)-hydroxyl-1,6-dihydropurine riboside, a reaction coordinate analogue, have been determined and refined to resolutions of 2.6 and 1.95 A, respectively. Crystals of both complexes were obtained at pH 7, where the, enzyme is fully active, in an identical space group with the asymmetric, unit containing four molecules. In addition to the very high degree of, similarity between the four ... [(full description)]
About this StructureAbout this Structure
1A4L is a [Single protein] structure of sequence from [Mus musculus] with ZN and DCF as [ligands]. Active as [Adenosine deaminase], with EC number [3.5.4.4]. Structure known Active Site: . Full crystallographic information is available from [OCA].
ReferenceReference
Complexes of adenosine deaminase with two potent inhibitors: X-ray structures in four independent molecules at pH of maximum activity., Wang Z, Quiocho FA, Biochemistry. 1998 Jun 9;37(23):8314-24. PMID:9622483
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