Copper in PDB 6gby: Copper Nitrite Reductase From Achromobacter Cycloclastes: Non- Polymorph Separated Dataset 1

All present enzymatic activity of Copper Nitrite Reductase From Achromobacter Cycloclastes: Non- Polymorph Separated Dataset 1:
1.7.2.1;

The structure of Copper Nitrite Reductase From Achromobacter Cycloclastes: Non- Polymorph Separated Dataset 1, PDB code: 6gby was solved by A.Ebrahim, M.V.Appleby, D.Axford, J.Beale, T.Moreno-Chicano, D.A.Sherrell, R.W.Strange, R.L.Owen, M.A.Hough, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	29.21 / 1.48
Space group	P 21 3
Cell size a, b, c (Å), α, β, γ (°)	96.870, 96.870, 96.870, 90.00, 90.00, 90.00
R / Rfree (%)	23.5 / 27.6

The binding sites of Copper atom in the Copper Nitrite Reductase From Achromobacter Cycloclastes: Non- Polymorph Separated Dataset 1 (pdb code 6gby). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total 2 binding sites of Copper where determined in the Copper Nitrite Reductase From Achromobacter Cycloclastes: Non- Polymorph Separated Dataset 1, PDB code: 6gby:
Jump to Copper binding site number: 1; 2;

Copper binding site 1 out of 2 in the Copper Nitrite Reductase From Achromobacter Cycloclastes: Non- Polymorph Separated Dataset 1


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of Copper Nitrite Reductase From Achromobacter Cycloclastes: Non- Polymorph Separated Dataset 1 within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu501 b:25.2 occ:1.00 ND1 A:HIS95 2.2 21.8 1.0 SG A:CYS136 2.3 23.6 1.0 SD A:MET150 2.3 20.1 1.0 CD2 A:HIS145 2.3 20.7 1.0 CE A:MET150 3.1 21.2 1.0 CG A:HIS145 3.1 20.8 1.0 CE1 A:HIS95 3.2 21.0 1.0 CB A:CYS136 3.2 21.8 1.0 CG A:HIS95 3.2 23.0 1.0 NE2 A:HIS145 3.4 21.3 1.0 CB A:HIS95 3.5 22.4 1.0 CB A:HIS145 3.5 20.5 1.0 CG A:MET150 3.9 19.2 1.0 CA A:HIS95 3.9 24.0 1.0 ND1 A:HIS145 4.3 22.5 1.0 NE2 A:HIS95 4.3 21.4 1.0 CD2 A:HIS95 4.3 22.4 1.0 CG A:PRO138 4.4 26.0 1.0 O A:LEU94 4.4 24.6 1.0 CE1 A:HIS145 4.4 21.5 1.0 CB A:MET150 4.4 17.8 1.0 SD A:MET62 4.6 22.8 1.0 N A:ASN96 4.6 23.7 1.0 CA A:CYS136 4.7 20.1 1.0 CA A:HIS145 4.7 19.1 1.0 CD A:PRO138 4.8 26.3 1.0 C A:HIS95 4.9 24.6 1.0 CB A:MET62 4.9 22.7 1.0 N A:HIS95 5.0 25.0 1.0

Copper binding site 2 out of 2 in the Copper Nitrite Reductase From Achromobacter Cycloclastes: Non- Polymorph Separated Dataset 1


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 2 of Copper Nitrite Reductase From Achromobacter Cycloclastes: Non- Polymorph Separated Dataset 1 within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu502 b:18.5 occ:1.00 O2 A:NO2503 2.0 22.6 1.0 NE2 A:HIS100 2.0 15.0 1.0 NE2 A:HIS135 2.1 19.5 1.0 N A:NO2503 2.1 25.3 1.0 O1 A:NO2503 2.3 21.7 1.0 CE1 A:HIS100 2.9 16.2 1.0 CE1 A:HIS135 3.0 18.5 1.0 CD2 A:HIS100 3.1 15.2 1.0 CD2 A:HIS135 3.2 18.4 1.0 ND1 A:HIS100 4.1 15.4 1.0 ND1 A:HIS135 4.1 18.9 1.0 OD2 A:ASP98 4.1 28.5 1.0 CG A:HIS100 4.2 15.5 1.0 CG A:HIS135 4.3 18.2 1.0 CG A:ASP98 4.6 24.8 1.0 OD1 A:ASP98 4.8 25.7 1.0

A.Ebrahim, M.V.Appleby, D.Axford, J.Beale, T.Moreno-Chicano, D.A.Sherrell, R.W.Strange, M.A.Hough, R.L.Owen. Resolving Polymorphs and Radiation-Driven Effects in Microcrystals Using Fixed-Target Serial Synchrotron Crystallography. Acta Crystallogr D Struct V. 75 151 2019BIOL.
ISSN: ISSN 2059-7983
PubMed: 30821704
DOI: 10.1107/S2059798318010240