4zkl | pdb_00004zkl

Crystal structure of human histidine triad nucleotide-binding protein 1 (hHINT1) complexed with JB419 (AP4A analog)

spinqualitylabelsall models 4zkl, resolution 2.34Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4zkl is a 4 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 2.34Å Ligands: AMP, JB6 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 Histidine triad nucleotide-binding protein 1 (HINT1) represents the most ancient and widespread branch in the histidine triad proteins superfamily. HINT1 plays an important role in various biological processes, and it has been found in many species. Here, we report the first structure (at a 2.34A resolution) of a complex of human HINT1 with a non-hydrolyzable analog of an Ap4A dinucleotide, containing bis-phosphorothioated glycerol mimicking a polyphosphate chain, obtained from a primitive monoclinic space group P21 crystal. In addition, the apo form of hHINT1 at the space group P21 refined to 1.92A is reported for comparative studies. Crystallographic studies of the complex of human HINT1 protein with a non-hydrolyzable analog of ApA.,Dolot R, Kaczmarek R, Seda A, Krakowiak A, Baraniak J, Nawrot B Int J Biol Macromol. 2016 Feb 18;87:62-69. doi: 10.1016/j.ijbiomac.2016.02.047. PMID:26905466 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Histidine triad nucleotide-binding protein 3D structures

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