Copper in PDB 6zua: Cu Nitrite Reductase From Achromobacter Cycloclastes: Msox Series at 170K, Dose Point 4

All present enzymatic activity of Cu Nitrite Reductase From Achromobacter Cycloclastes: Msox Series at 170K, Dose Point 4:
1.7.2.1;

The structure of Cu Nitrite Reductase From Achromobacter Cycloclastes: Msox Series at 170K, Dose Point 4, PDB code: 6zua was solved by M.A.Hough, S.V.Antonyuk, R.W.Strange, S.S.Hasnain, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	42.68 / 1.14
Space group	P 21 3
Cell size a, b, c (Å), α, β, γ (°)	95.35, 95.35, 95.35, 90, 90, 90
R / Rfree (%)	n/a / n/a

The binding sites of Copper atom in the Cu Nitrite Reductase From Achromobacter Cycloclastes: Msox Series at 170K, Dose Point 4 (pdb code 6zua). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total 2 binding sites of Copper where determined in the Cu Nitrite Reductase From Achromobacter Cycloclastes: Msox Series at 170K, Dose Point 4, PDB code: 6zua:
Jump to Copper binding site number: 1; 2;

Copper binding site 1 out of 2 in the Cu Nitrite Reductase From Achromobacter Cycloclastes: Msox Series at 170K, Dose Point 4


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of Cu Nitrite Reductase From Achromobacter Cycloclastes: Msox Series at 170K, Dose Point 4 within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu401 b:10.2 occ:1.00 ND1 A:HIS145 2.1 9.2 1.0 ND1 A:HIS95 2.1 8.6 1.0 SG A:CYS136 2.2 9.7 1.0 SD A:MET150 2.6 11.5 1.0 CE1 A:HIS145 2.9 9.2 1.0 CE1 A:HIS95 3.0 8.9 1.0 CG A:HIS145 3.1 9.0 1.0 CG A:HIS95 3.1 8.0 1.0 CB A:CYS136 3.2 8.7 1.0 CE A:MET150 3.3 11.8 1.0 CB A:HIS95 3.5 8.8 1.0 CB A:HIS145 3.5 9.5 1.0 CA A:HIS95 3.8 7.9 1.0 CG A:MET150 4.0 13.8 1.0 NE2 A:HIS145 4.1 9.4 1.0 CD2 A:HIS145 4.2 12.0 1.0 NE2 A:HIS95 4.2 8.8 1.0 O A:LEU94 4.2 11.2 1.0 CD2 A:HIS95 4.2 8.2 1.0 CG A:PRO138 4.2 14.6 1.0 CB A:MET150 4.4 10.3 1.0 SD A:MET62 4.5 12.8 1.0 CD A:PRO138 4.6 9.3 1.0 CA A:CYS136 4.6 7.0 1.0 N A:ASN96 4.7 8.5 1.0 CA A:HIS145 4.7 8.2 1.0 N A:HIS95 4.8 8.3 1.0 C A:HIS95 4.9 8.4 1.0 C A:LEU94 4.9 9.2 1.0

Copper binding site 2 out of 2 in the Cu Nitrite Reductase From Achromobacter Cycloclastes: Msox Series at 170K, Dose Point 4


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 2 of Cu Nitrite Reductase From Achromobacter Cycloclastes: Msox Series at 170K, Dose Point 4 within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu402 b:8.3 occ:0.80 O A:NO407 1.6 20.1 0.3 O A:HOH808 1.8 8.5 0.3 N A:NO407 1.9 19.2 0.3 NE2 A:HIS100 2.0 8.3 1.0 NE2 A:HIS135 2.0 9.8 1.0 O2 A:NO2404 2.1 19.2 0.4 N A:NO2404 2.5 18.0 0.4 O1 A:NO2404 2.7 19.0 0.4 CE1 A:HIS100 2.9 8.1 1.0 CD2 A:HIS135 3.0 9.0 1.0 CE1 A:HIS135 3.0 8.6 1.0 CD2 A:HIS100 3.1 7.3 1.0 OD2 A:ASP98 3.6 13.7 0.7 ND1 A:HIS100 4.1 7.4 1.0 ND1 A:HIS135 4.1 8.3 1.0 CG A:HIS135 4.1 7.2 1.0 CG A:HIS100 4.2 7.4 1.0 CG A:ASP98 4.3 10.4 0.7 OD1 A:ASP98 4.6 10.4 0.7 O A:HOH991 4.6 25.4 0.5 OD2 A:ASP98 4.9 12.7 0.3

M.A.Hough, J.Conradie, R.W.Strange, S.V.Antonyuk, R.R.Eady, A.Ghosh, S.S.Hasnain. Nature of the Copper-Nitrosyl Intermediates of Copper Nitrite Reductases During Catalysis. Chem Sci V. 11 12485 2020.
ISSN: ISSN 2041-6520
PubMed: 34094452
DOI: 10.1039/D0SC04797J