Copper in PDB 1rcy: Rusticyanin (Rc) From Thiobacillus Ferrooxidans

The structure of Rusticyanin (Rc) From Thiobacillus Ferrooxidans, PDB code: 1rcy was solved by R.L.Walter, A.M.Friedman, S.E.Ealick, R.C.Blake Ii, P.Proctor, M.Shoham, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	10.00 / 1.90
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	32.510, 60.670, 38.140, 90.00, 108.42, 90.00
R / Rfree (%)	17.5 / 25.2

The binding sites of Copper atom in the Rusticyanin (Rc) From Thiobacillus Ferrooxidans (pdb code 1rcy). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total only one binding site of Copper was determined in the Rusticyanin (Rc) From Thiobacillus Ferrooxidans, PDB code: 1rcy:

Copper binding site 1 out of 1 in the Rusticyanin (Rc) From Thiobacillus Ferrooxidans


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of Rusticyanin (Rc) From Thiobacillus Ferrooxidans within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu156 b:13.3 occ:1.00 ND1 A:HIS143 1.9 8.0 1.0 ND1 A:HIS85 2.0 9.8 1.0 SG A:CYS138 2.3 7.0 1.0 CE1 A:HIS143 2.8 9.6 1.0 SD A:MET148 2.9 7.8 1.0 CG A:HIS143 3.0 9.3 1.0 CE1 A:HIS85 3.0 10.1 1.0 CG A:HIS85 3.1 8.6 1.0 CB A:CYS138 3.2 7.1 1.0 CB A:HIS85 3.4 9.3 1.0 CB A:HIS143 3.4 9.1 1.0 CE A:MET148 3.7 6.1 1.0 CA A:HIS85 3.8 8.9 1.0 NE2 A:HIS143 4.0 9.8 1.0 CD1 A:ILE140 4.0 16.0 1.0 CB A:ILE140 4.1 9.2 1.0 CD2 A:HIS143 4.1 9.9 1.0 NE2 A:HIS85 4.2 10.1 1.0 CG1 A:ILE140 4.2 9.4 1.0 CD2 A:HIS85 4.2 9.7 1.0 CG A:MET148 4.4 5.1 1.0 CA A:CYS138 4.6 6.1 1.0 N A:HIS85 4.7 9.4 1.0 N A:SER86 4.8 8.4 1.0 N A:ILE140 4.9 11.1 1.0 CB A:PRO52 4.9 15.8 1.0 CB A:MET148 4.9 6.8 1.0 C A:HIS85 4.9 9.5 1.0 CA A:HIS143 4.9 10.3 1.0 CG2 A:ILE140 5.0 7.5 1.0

R.L.Walter, S.E.Ealick, A.M.Friedman, R.C.Blake 2Nd., P.Proctor, M.Shoham. Multiple Wavelength Anomalous Diffraction (Mad) Crystal Structure of Rusticyanin: A Highly Oxidizing Cupredoxin with Extreme Acid Stability. J.Mol.Biol. V. 263 730 1996.
ISSN: ISSN 0022-2836
PubMed: 8947572
DOI: 10.1006/JMBI.1996.0612