Fig. 5: Structures of Cu-containing RbAng-1a.
From: Signal-strapping as a protein-sequence search method for the discovery of metalloproteins
a overall protein structure showing secondary structural elements, Van der Waals’ surface (light grey) and amino acid residues molecules coordinating to the copper ion (green coloured cylinders); b Electron density at 1.0 RMSD for the metal-binding site of RbAng-1a. Cu+ centre is in brown. c Distances of the Cu centre to nitrogens in His1 and oxygen from Asn41. d X-band, CW-EPR spectrum (150 K) of Cu2+-RbAng-1a. e Electronic environment surrounding the metal-binding site of RbAng-1a generated by the APBS53 plugin for PyMol50 settled at pH 7.0 to calculate and visualise the surface electrostatic potential at ± 2 KBT/e. This analysis showed that the top flat surface harbouring the active site is negatively charged. Cu+ centre is in brown. f The conservation of the His1 is displayed by the Consurf55 analysis, further emphasising the importance of the mono-histidine brace within this herein identified metalloprotein family. However, the surrounding amino acids are not highly conserved, even the coordinating asparagine 41. Cu+ centre is in brown. Source data are provided as a Source Data file.
