Copper in PDB 6f1q: Crystal Structure of Three-Domain Heme-Cu Nitrite Reductase From Ralstonia Pickettii in I213 Space Group

All present enzymatic activity of Crystal Structure of Three-Domain Heme-Cu Nitrite Reductase From Ralstonia Pickettii in I213 Space Group:
1.7.2.1;

The structure of Crystal Structure of Three-Domain Heme-Cu Nitrite Reductase From Ralstonia Pickettii in I213 Space Group, PDB code: 6f1q was solved by S.Antonyuk, D.Sasaki, R.R.Eady, S.S.Hasnain, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	50.00 / 2.30
Space group	I 21 3
Cell size a, b, c (Å), α, β, γ (°)	180.853, 180.853, 180.853, 90.00, 90.00, 90.00
R / Rfree (%)	13.4 / 16.2

The structure of Crystal Structure of Three-Domain Heme-Cu Nitrite Reductase From Ralstonia Pickettii in I213 Space Group also contains other interesting chemical elements:

Iron

(Fe)

1 atom

The binding sites of Copper atom in the Crystal Structure of Three-Domain Heme-Cu Nitrite Reductase From Ralstonia Pickettii in I213 Space Group (pdb code 6f1q). 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 Three-Domain Heme-Cu Nitrite Reductase From Ralstonia Pickettii in I213 Space Group, PDB code: 6f1q:
Jump to Copper binding site number: 1; 2;

Copper binding site 1 out of 2 in the Crystal Structure of Three-Domain Heme-Cu Nitrite Reductase From Ralstonia Pickettii in I213 Space Group


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 Three-Domain Heme-Cu Nitrite Reductase From Ralstonia Pickettii in I213 Space Group within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu501 b:38.8 occ:1.00 ND1 A:HIS143 2.0 34.0 1.0 ND1 A:HIS94 2.1 39.7 1.0 SG A:CYS135 2.2 38.6 1.0 SD A:MET148 2.6 40.4 1.0 CE1 A:HIS143 2.9 38.7 1.0 CE1 A:HIS94 3.1 43.2 1.0 CG A:HIS143 3.1 37.0 1.0 CG A:HIS94 3.1 35.7 1.0 CB A:CYS135 3.2 37.3 1.0 CE A:MET148 3.3 38.9 1.0 CB A:HIS94 3.5 39.0 1.0 CB A:HIS143 3.5 39.5 1.0 CA A:HIS94 3.8 36.4 1.0 O A:PRO93 4.0 36.7 1.0 NE2 A:HIS143 4.1 33.2 1.0 CG A:MET148 4.1 38.8 1.0 CD2 A:HIS143 4.1 35.4 1.0 NE2 A:HIS94 4.2 40.1 1.0 CD2 A:HIS94 4.2 42.4 1.0 CB A:THR137 4.4 38.4 1.0 OG1 A:THR137 4.4 39.3 1.0 CE3 A:TRP61 4.5 35.7 1.0 N A:ASN95 4.6 35.0 1.0 CA A:HIS143 4.6 36.5 1.0 CB A:MET148 4.7 36.2 1.0 CA A:CYS135 4.7 35.7 1.0 N A:HIS94 4.7 36.2 1.0 C A:HIS94 4.8 37.7 1.0 C A:PRO93 4.8 37.1 1.0

Copper binding site 2 out of 2 in the Crystal Structure of Three-Domain Heme-Cu Nitrite Reductase From Ralstonia Pickettii in I213 Space Group


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 Three-Domain Heme-Cu Nitrite Reductase From Ralstonia Pickettii in I213 Space Group within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu502 b:38.7 occ:1.00 NE2 A:HIS99 1.9 28.7 1.0 NE2 A:HIS134 2.1 33.5 1.0 O A:HOH637 2.2 42.6 1.0 CE1 A:HIS99 2.8 32.5 1.0 CD2 A:HIS134 2.9 33.5 1.0 CD2 A:HIS99 3.0 34.1 1.0 CE1 A:HIS134 3.2 35.8 1.0 OD2 A:ASP97 4.0 37.0 1.0 ND1 A:HIS99 4.0 31.1 1.0 CG A:HIS99 4.1 31.0 1.0 CG A:HIS134 4.1 34.5 1.0 ND1 A:HIS134 4.2 35.4 1.0 O A:HOH688 4.5 65.7 1.0 CG A:ASP97 4.5 38.9 1.0 OD1 A:ASP97 4.9 39.2 1.0

J.Dong, D.Sasaki, R.Eady, S.V.Antonyuk, S.S.Hasnain. Substrate Entry and Binding Requires Activation of Tyrosine in Heme-Copper Nitrite Reductase To Be Published.