3TW2

High resolution structure of human histidine triad nucleotide-binding protein 1 (hHINT1)/AMP complex in a monoclinic space group

Summary for 3TW2

• Entry DOI: 10.2210/pdb3tw2/pdb
• Related: 1AV5 1KPA 1KPB 1KPC 1KPE 1KPF
• Descriptor: Histidine triad nucleotide-binding protein 1, ADENOSINE MONOPHOSPHATE (3 entities in total)
• Functional Keywords: hydrolase
• Biological source: Homo sapiens (human)
• Cellular location: Cytoplasm: P49773
• Total number of polymer chains: 2
• Total formula weight: 27995.08

Authors

Dolot, R.M.,Wlodarczyk, A.,Ozga, M.,Krakowiak, A.,Nawrot, B. (deposition date: 2011-09-21, release date: 2011-11-02, Last modification date: 2023-09-13)

Primary citation

Dolot, R.,Ozga, M.,Wlodarczyk, A.,Krakowiak, A.,Nawrot, B.
A new crystal form of human histidine triad nucleotide-binding protein 1 (hHINT1) in complex with adenosine 5'-monophosphate at 1.38 A resolution.
Acta Crystallogr.,Sect.F, 68:883-888, 2012

PubMed Abstract: Histidine triad nucleotide-binding protein 1 (HINT1) represents the most ancient and widespread branch of the histidine triad protein superfamily. HINT1 plays an important role in various biological processes and has been found in many species. Here, the structure of the human HINT1-adenosine 5'-monophosphate (AMP) complex at 1.38 Å resolution obtained from a new monoclinic crystal form is reported. The final structure has R(cryst) = 0.1207 (R(free) = 0.1615) and the model exhibits good stereochemical quality. Detailed analysis of the high-resolution data allowed the details of the protein structure to be updated in comparison to the previously published data.

PubMed: 22869114
DOI: 10.1107/S1744309112029491

Experimental method

X-RAY DIFFRACTION (1.38 Å)