Structural highlights
3qgz is a 1 chain structure with sequence from European rabbit. This structure supersedes the now removed PDB entry 3llj. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
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| Ligands: | |
| Related: | 3llj, 1rzy, 3rhn, 4rhn, 5rhn, 6rhn |
| Gene: | HINT1, HINT (European rabbit) |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
[HINT1_RABIT] Hydrolyzes adenosine 5'-monophosphoramidate substrates such as AMP-morpholidate, AMP-N-alanine methyl ester, AMP-alpha-acetyl lysine methyl ester and AMP-NH2.
Publication Abstract from PubMed
Histidine triad nucleotide-binding protein 1 (HINT1) represents the most ancient and widespread branch in the histidine-triad protein superfamily. HINT1 plays an important role in various biological processes and has been found in many species. Here, the first complete structure of the rabbit HINT1-adenosine complex is reported at 1.10 A resolution, which is one of the highest resolutions obtained for a HINT1 structure. The final structure has an R(cryst) of 14.25% (R(free) = 16.77%) and the model exhibits good stereochemical qualities. A detailed analysis of the atomic resolution data allowed an update of the details of the protein structure in comparison to previously published data.
High-resolution X-ray structure of the rabbit histidine triad nucleotide-binding protein 1 (rHINT1)-adenosine complex at 1.10 A resolution.,Dolot R, Ozga M, Krakowiak A, Nawrot B Acta Crystallogr D Biol Crystallogr. 2011 Jul;67(Pt 7):601-7. doi:, 10.1107/S0907444911015605. Epub 2011 Jun 14. PMID:21697598[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Dolot R, Ozga M, Krakowiak A, Nawrot B. High-resolution X-ray structure of the rabbit histidine triad nucleotide-binding protein 1 (rHINT1)-adenosine complex at 1.10 A resolution. Acta Crystallogr D Biol Crystallogr. 2011 Jul;67(Pt 7):601-7. doi:, 10.1107/S0907444911015605. Epub 2011 Jun 14. PMID:21697598 doi:10.1107/S0907444911015605
