Copper in PDB 3zbm: Structure of M92A Variant of Three-Domain Heme-Cu Nitrite Reductase From Ralstonia Pickettii

All present enzymatic activity of Structure of M92A Variant of Three-Domain Heme-Cu Nitrite Reductase From Ralstonia Pickettii:
1.7.2.1;

The structure of Structure of M92A Variant of Three-Domain Heme-Cu Nitrite Reductase From Ralstonia Pickettii, PDB code: 3zbm was solved by S.V.Antonyuk, C.Han, 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)	40.14 / 1.87
Space group	H 3
Cell size a, b, c (Å), α, β, γ (°)	128.410, 128.410, 86.090, 90.00, 90.00, 120.00
R / Rfree (%)	13.9 / 16.8

The structure of Structure of M92A Variant of 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 Structure of M92A Variant of Three-Domain Heme-Cu Nitrite Reductase From Ralstonia Pickettii (pdb code 3zbm). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total 2 binding sites of Copper where determined in the Structure of M92A Variant of Three-Domain Heme-Cu Nitrite Reductase From Ralstonia Pickettii, PDB code: 3zbm:
Jump to Copper binding site number: 1; 2;

Copper binding site 1 out of 2 in the Structure of M92A Variant of 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 Structure of M92A Variant of Three-Domain Heme-Cu Nitrite Reductase From Ralstonia Pickettii within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu1460 b:19.9 occ:1.00 ND1 A:HIS94 2.0 16.0 1.0 ND1 A:HIS143 2.1 18.8 1.0 SG A:CYS135 2.2 19.4 1.0 SD A:MET148 2.6 22.9 1.0 CE1 A:HIS143 2.9 19.6 1.0 CE1 A:HIS94 3.0 18.4 1.0 CG A:HIS94 3.1 18.5 1.0 CG A:HIS143 3.1 17.6 1.0 CB A:CYS135 3.1 18.9 1.0 CB A:HIS94 3.4 19.8 1.0 CE A:MET148 3.4 18.9 1.0 CB A:HIS143 3.5 17.7 1.0 CA A:HIS94 3.8 19.6 1.0 O A:PRO93 4.0 17.7 1.0 NE2 A:HIS143 4.1 20.7 1.0 NE2 A:HIS94 4.1 15.5 1.0 CD2 A:HIS94 4.2 17.9 1.0 CD2 A:HIS143 4.2 20.2 1.0 CG A:MET148 4.2 19.7 1.0 OG1 A:THR137 4.3 20.4 1.0 CB A:THR137 4.3 21.6 1.0 CE3 A:TRP61 4.5 20.7 1.0 N A:ASN95 4.6 18.9 1.0 CA A:CYS135 4.6 17.7 1.0 CA A:HIS143 4.6 18.6 1.0 CB A:MET148 4.7 17.6 1.0 C A:HIS94 4.8 19.2 1.0 N A:HIS94 4.8 19.2 1.0 C A:PRO93 4.8 19.4 1.0 CZ3 A:TRP61 4.9 20.5 1.0

Copper binding site 2 out of 2 in the Structure of M92A Variant of 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 Structure of M92A Variant of Three-Domain Heme-Cu Nitrite Reductase From Ralstonia Pickettii within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu1461 b:23.3 occ:1.00 O A:HOH2136 1.9 31.8 1.0 NE2 A:HIS99 2.0 17.9 1.0 NE2 A:HIS134 2.0 17.0 1.0 CD2 A:HIS134 2.9 19.5 1.0 CE1 A:HIS99 3.0 19.6 1.0 CD2 A:HIS99 3.1 17.3 1.0 CE1 A:HIS134 3.1 19.3 1.0 OD2 A:ASP97 3.8 25.1 1.0 CG A:HIS134 4.1 16.1 1.0 ND1 A:HIS99 4.1 16.3 1.0 CG A:HIS99 4.2 17.6 1.0 ND1 A:HIS134 4.2 16.3 1.0 CG A:ASP97 4.4 23.1 1.0 OD1 A:ASP97 4.8 23.8 1.0

S.V.Antonyuk, C.Han, R.R.Eady, S.S.Hasnain. Structures of Protein-Protein Complexes Involved in Electron Transfer. Nature V. 496 123 2013.
ISSN: ESSN 1476-4687
PubMed: 23535590
DOI: 10.1038/NATURE11996