Copper in PDB 6thf: Crystal Structure of Two-Domain Cu Nitrite Reductase From Bradyrhizobium Sp. Ors 375

All present enzymatic activity of Crystal Structure of Two-Domain Cu Nitrite Reductase From Bradyrhizobium Sp. Ors 375:
1.7.2.1;

The structure of Crystal Structure of Two-Domain Cu Nitrite Reductase From Bradyrhizobium Sp. Ors 375, PDB code: 6thf was solved by D.Sasaki, T.F.Watanabe, R.R.Eady, R.C.Garratt, S.V.Antonyuk, S.S.Hasnain, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	50.93 / 1.47
Space group	P 21 3
Cell size a, b, c (Å), α, β, γ (°)	106.929, 106.929, 106.929, 90.00, 90.00, 90.00
R / Rfree (%)	14.1 / 15.7

The binding sites of Copper atom in the Crystal Structure of Two-Domain Cu Nitrite Reductase From Bradyrhizobium Sp. Ors 375 (pdb code 6thf). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total 2 binding sites of Copper where determined in the Crystal Structure of Two-Domain Cu Nitrite Reductase From Bradyrhizobium Sp. Ors 375, PDB code: 6thf:
Jump to Copper binding site number: 1; 2;

Copper binding site 1 out of 2 in the Crystal Structure of Two-Domain Cu Nitrite Reductase From Bradyrhizobium Sp. Ors 375


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of Crystal Structure of Two-Domain Cu Nitrite Reductase From Bradyrhizobium Sp. Ors 375 within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu411 b:15.5 occ:1.00 ND1 A:HIS140 2.0 16.3 1.0 ND1 A:HIS89 2.1 13.2 1.0 SG A:CYS130 2.2 15.1 1.0 SD A:MET145 2.5 15.3 1.0 CE1 A:HIS89 2.9 15.6 1.0 CE1 A:HIS140 3.0 15.8 1.0 CG A:HIS140 3.1 15.6 1.0 CG A:HIS89 3.1 14.8 1.0 CB A:CYS130 3.2 13.7 1.0 CE A:MET145 3.3 14.7 1.0 CB A:HIS140 3.5 14.7 1.0 CB A:HIS89 3.5 14.0 1.0 CA A:HIS89 3.8 14.6 1.0 CG A:MET145 4.0 14.3 1.0 NE2 A:HIS140 4.1 17.0 1.0 NE2 A:HIS89 4.1 15.2 1.0 O A:PRO88 4.1 17.0 1.0 CD2 A:HIS140 4.2 16.8 1.0 CG A:PRO132 4.2 16.0 0.7 CD2 A:HIS89 4.2 14.2 1.0 CG A:PRO132 4.2 15.6 0.3 CB A:MET145 4.4 13.8 1.0 SD A:MET56 4.6 13.2 0.3 CA A:CYS130 4.6 14.7 1.0 CD A:PRO132 4.6 15.0 0.7 N A:ASN90 4.6 14.3 1.0 CD A:PRO132 4.7 15.2 0.3 CA A:HIS140 4.7 14.3 1.0 N A:HIS89 4.8 15.6 1.0 C A:HIS89 4.8 15.2 1.0 C A:PRO88 4.9 16.3 1.0 CE A:MET56 4.9 18.0 0.7

Copper binding site 2 out of 2 in the Crystal Structure of Two-Domain Cu Nitrite Reductase From Bradyrhizobium Sp. Ors 375


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 2 of Crystal Structure of Two-Domain Cu Nitrite Reductase From Bradyrhizobium Sp. Ors 375 within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu412 b:13.1 occ:0.85 O A:HOH509 1.8 20.3 1.0 NE2 A:HIS94 2.0 12.8 1.0 NE2 A:HIS129 2.0 14.0 1.0 CE1 A:HIS94 3.0 12.5 1.0 CD2 A:HIS129 3.0 13.4 1.0 CD2 A:HIS94 3.1 12.9 1.0 CE1 A:HIS129 3.1 13.2 1.0 OD2 A:ASP92 3.7 19.7 1.0 O A:HOH872 3.9 22.1 0.5 ND1 A:HIS94 4.1 12.5 1.0 CG A:HIS129 4.1 12.8 1.0 ND1 A:HIS129 4.2 13.7 1.0 CG A:HIS94 4.2 12.1 1.0 CG A:ASP92 4.3 17.4 1.0 OD1 A:ASP92 4.5 16.7 1.0 O A:HOH687 4.8 16.5 1.0

D.Sasaki, T.F.Watanabe, R.R.Eady, R.C.Garratt, S.V.Antonyuk, S.S.Hasnain. Reverse Protein Engineering of A Novel 4-Domain Copper Nitrite Reductase Reveals Functional Regulation By Protein-Protein Interaction. Febs J. 2020.
ISSN: ISSN 1742-464X
PubMed: 32255260
DOI: 10.1111/FEBS.15324