Fig. 3: Structure and depictions of Cu-containing DUF6702.

a TSA of apo PaDUF6702a in the presence of several metals at 1:1 molar equivalent. Each TSA curve is coloured according with its respective metal-Cl₂ as shown in the figure legend. Positive shifts indicate ligand binding to the proteins and thermal stabilisation, while negative shifts indicate ligand binding to the proteins and thermal destabilisation due to protein aggregation or precipitation. b Overlapped Apo-, Co- and Cu-forms modelled structures of PaDUF6702a, showing secondary structural elements coloured by the pLDDT scores; Van der Waals’ surface (light grey). Cu²⁺ centre is coloured in brown and cobalt centre coloured in light pink c. Metal binding site of non-canonical tri-histidine brace from PaDUF6702. Cu²⁺ centre is coloured by the pLDDT score. d EPR spectra from PaDUF6702 at pH 7.0. e Electrostatic surface potential of PaDUF6702a generated by the APBS plugin for PyMol settled at pH 7.0 to calculate and visualise the surface electrostatic potential at ± 2 K_BT/e. The Cu²⁺ centre is coloured in brown. f Sequence conservation analysis (ConSurf) of PaDUF6702a coloured by the ConSurf score. The Cu²⁺ centre is coloured brown. Source data are provided as a Source Data file.