9qtc

HINT1 complexed with GS-441524

spinqualitylabelsall models 9qtc, resolution 1.30Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 9qtc is a 2 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.3Å Ligands: MES, U08 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function HINT1_HUMAN Hydrolyzes adenosine 5'-monophosphoramidate substrates such as AMP-morpholidate, AMP-N-alanine methyl ester, AMP-alpha-acetyl lysine methyl ester and AMP-NH2 (By similarity). Publication Abstract from PubMed Remdesivir is an antiviral ProTide-type nucleotide analog, which is activated into its 5'-triphosphate form by several cellular enzymes. The human histidine triad nucleotide-binding protein 1 (hHINT1) hydrolyzes the P-N bond to release the 5'-monophosphate. The nucleotide chemical structure consequently impacts the activation pathway efficacy. We report crystal structures of human HINT1 in complex with either the nucleoside GS-441524 or the monophosphate nucleoside GS-441524-MP-both metabolites of remdesivir at 1.30 A and 1.58 A resolution, respectively. Together with enzymatic data, these results disclose the main structural determinants governing activity, namely the steric hindrance of the phosphoramidate moiety as well as ribose modifications altering interactions with Asp43. Impact of remdesivir modifications on human HINT1 binding - A structural and functional study in the remdesivir activation pathway.,Chazot A, Zimberger C, Fotopoulos I, Canard B, Alvarez K, Ferron F Structure. 2026 May 25:S0969-2126(26)00146-2. doi: 10.1016/j.str.2026.04.015. PMID:42184828 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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