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6YQM

Human histidine triad nucleotide-binding protein 1 (hHINT1) complexed with dGMP and refined to 1.02 A

This is a non-PDB format compatible entry.
Summary for 6YQM
Entry DOI10.2210/pdb6yqm/pdb
Related3TW2
DescriptorHistidine triad nucleotide-binding protein 1, 2'-DEOXYGUANOSINE-5'-MONOPHOSPHATE, DI(HYDROXYETHYL)ETHER, ... (4 entities in total)
Functional Keywordsnucleotide binding protein, hydrolase
Biological sourceHomo sapiens (Human)
Total number of polymer chains2
Total formula weight28101.20
Authors
Dolot, R.D.,Seda, A.,Nawrot, B.C. (deposition date: 2020-04-17, release date: 2020-04-29, Last modification date: 2024-01-24)
Primary citationDolot, 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: 34329705
DOI: 10.1016/j.bbagen.2021.129968
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.02 Å)
Structure validation

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