{'fraction_non_alphanumeric': 0.022789425706472195, 'fraction_numerical': 0.004557885141294439, 'mean_word_length': 5.274285714285714, 'pattern_counts': {'":': 0, '<': 0, '<?xml version=': 0, '>': 0, 'https://': 0, 'lorem ipsum': 0, 'www.': 0, 'xml': 0}, 'pii_count': 0, 'substrings_counts': 0, 'word_list_counts': {'cursed_substrings.json': 0, 'profanity_word_list.json': 0, 'sexual_word_list.json': 0, 'zh_pornsignals.json': 0}}
Predicting the coordination number within copper chaperones: Atox1 as case study.

The concentration of copper ions in biological systems is tightly regulated by metallochaperone proteins which are responsible for Cu(I) delivery to designated locations in the cell. These proteins contain a unique motif (MXCXXC) that binds Cu(I) very tightly and specifically but at the same time allows efficient metal transfer to target proteins that often contain a similar copper binding motif. It was found that binding to Cu(I) is achieved through the two cysteine residues in a low coordination number of 2-3 due to possible binding of a third external ligand. Understanding copper transport requires better understanding of copper coordination. Here we therefore focused on establishing a computational method that can predict the coordination number of copper in copper chaperones. The method is shown to be successful in predicting the coordination of Cu(I) within the human copper chaperone (Atox1). Based on the results, a possible rationale for this unique Cu(I) dicoordination in Atox1 is suggested.