Copper in PDB 5ocf: Crystal Structure of Nitric Oxide Bound to Three-Domain Heme-Cu Nitrite Reductase From Ralstonia Pickettii

The structure of Crystal Structure of Nitric Oxide Bound to Three-Domain Heme-Cu Nitrite Reductase From Ralstonia Pickettii, PDB code: 5ocf was solved by J.Dong, D.Sasaki, R.Eady, 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)	74.78 / 1.80
Space group	I 21 3
Cell size a, b, c (Å), α, β, γ (°)	183.180, 183.180, 183.180, 90.00, 90.00, 90.00
R / Rfree (%)	14.9 / 16.4

The structure of Crystal Structure of Nitric Oxide Bound to Three-Domain Heme-Cu Nitrite Reductase From Ralstonia Pickettii also contains other interesting chemical elements:

Iron

(Fe)

1 atom

The binding sites of Copper atom in the Crystal Structure of Nitric Oxide Bound to Three-Domain Heme-Cu Nitrite Reductase From Ralstonia Pickettii (pdb code 5ocf). 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 Nitric Oxide Bound to Three-Domain Heme-Cu Nitrite Reductase From Ralstonia Pickettii, PDB code: 5ocf:
Jump to Copper binding site number: 1; 2;

Copper binding site 1 out of 2 in the Crystal Structure of Nitric Oxide Bound to Three-Domain Heme-Cu Nitrite Reductase From Ralstonia Pickettii


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 Nitric Oxide Bound to Three-Domain Heme-Cu Nitrite Reductase From Ralstonia Pickettii within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu501 b:20.6 occ:1.00 ND1 A:HIS143 2.1 19.6 1.0 ND1 A:HIS94 2.2 20.3 1.0 SG A:CYS135 2.2 19.6 1.0 SD A:MET148 2.6 20.0 1.0 CE1 A:HIS143 3.0 20.0 1.0 CE1 A:HIS94 3.1 20.8 1.0 CG A:HIS143 3.1 19.1 1.0 CG A:HIS94 3.2 20.8 1.0 CB A:CYS135 3.2 19.6 1.0 CE A:MET148 3.4 20.7 1.0 CB A:HIS94 3.5 21.3 1.0 CB A:HIS143 3.5 18.7 1.0 CA A:HIS94 3.8 21.2 1.0 O A:PRO93 4.1 20.9 1.0 NE2 A:HIS143 4.1 19.4 1.0 CG A:MET148 4.2 19.4 1.0 CD2 A:HIS143 4.2 19.4 1.0 NE2 A:HIS94 4.2 21.1 1.0 CD2 A:HIS94 4.3 20.4 1.0 CB A:THR137 4.4 19.9 1.0 OG1 A:THR137 4.4 19.6 1.0 CE3 A:TRP61 4.6 19.8 1.0 N A:ASN95 4.6 19.2 1.0 CA A:HIS143 4.7 18.5 1.0 CA A:CYS135 4.7 18.6 1.0 CB A:MET148 4.7 18.6 1.0 C A:HIS94 4.8 21.5 1.0 N A:HIS94 4.8 21.1 1.0 C A:PRO93 4.8 20.7 1.0

Copper binding site 2 out of 2 in the Crystal Structure of Nitric Oxide Bound to Three-Domain Heme-Cu Nitrite Reductase From Ralstonia Pickettii


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 Nitric Oxide Bound to Three-Domain Heme-Cu Nitrite Reductase From Ralstonia Pickettii within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu502 b:21.8 occ:0.80 N A:NO504 2.0 17.6 0.8 NE2 A:HIS134 2.1 19.2 1.0 NE2 A:HIS99 2.2 18.7 1.0 O A:NO504 2.6 15.2 0.8 CD2 A:HIS134 3.0 19.2 1.0 CE1 A:HIS134 3.1 20.1 1.0 CE1 A:HIS99 3.1 18.6 1.0 CD2 A:HIS99 3.2 18.8 1.0 OD2 A:ASP97 3.8 22.3 1.0 CG A:HIS134 4.2 18.8 1.0 ND1 A:HIS134 4.2 19.7 1.0 ND1 A:HIS99 4.2 18.8 1.0 CG A:HIS99 4.3 18.3 1.0 CG A:ASP97 4.4 19.4 1.0 O A:HOH938 4.5 27.7 1.0 OD1 A:ASP97 4.7 18.6 1.0 O A:HOH997 4.8 22.1 0.6

J.Dong, D.Sasaki, R.Eady, S.V.Antonyuk, S.S.Hasnain. Activation of Redox Tyrosine Switch Is Required For Ligand Binding at the Catalytic Site in Heme-Cu Nitrite Reductases To Be Published.