6YVP
Human histidine triad nucleotide-binding protein 2 (hHINT2) complexed with dGMP and refined to 2.77 A
This is a non-PDB format compatible entry.
Summary for 6YVP
Entry DOI | 10.2210/pdb6yvp/pdb |
Related | 6YI0 6YPR 6YPX 6YQD |
Descriptor | Histidine triad nucleotide-binding protein 2, mitochondrial, 2'-DEOXYGUANOSINE-5'-MONOPHOSPHATE (3 entities in total) |
Functional Keywords | nucleotide binding protein, hydrolase |
Biological source | Homo sapiens (Human) |
Total number of polymer chains | 2 |
Total formula weight | 35061.89 |
Authors | Dolot, R.D.,Krakowiak, A.,Nawrot, B.C. (deposition date: 2020-04-28, release date: 2020-05-13, Last modification date: 2024-01-24) |
Primary citation | Dolot, R.,Krakowiak, A.,Kaczmarek, R.,Wlodarczyk, A.,Pichlak, M.,Nawrot, B. Biochemical, crystallographic and biophysical characterization of histidine triad nucleotide-binding protein 2 with different ligands including a non-hydrolyzable analog of Ap4A. Biochim Biophys Acta Gen Subj, 1865:129968-129968, 2021 Cited by PubMed Abstract: Human HINT2 is an important mitochondrial enzyme involved in many processes such as apoptosis and bioenergetics, but its endogenous substrates and the three-dimensional structure of the full-length protein have not been identified yet. PubMed: 34329705DOI: 10.1016/j.bbagen.2021.129968 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.77 Å) |
Structure validation
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