Copper in PDB 6gb8: Copper Nitrite Reductase From Achromobacter Cycloclastes: Small Cell Polymorph Dataset 1

All present enzymatic activity of Copper Nitrite Reductase From Achromobacter Cycloclastes: Small Cell Polymorph Dataset 1:
1.7.2.1;

The structure of Copper Nitrite Reductase From Achromobacter Cycloclastes: Small Cell Polymorph Dataset 1, PDB code: 6gb8 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)	29.06 / 1.48
Space group	P 21 3
Cell size a, b, c (Å), α, β, γ (°)	96.382, 96.382, 96.382, 90.00, 90.00, 90.00
R / Rfree (%)	18.6 / 21.6

The binding sites of Copper atom in the Copper Nitrite Reductase From Achromobacter Cycloclastes: Small Cell Polymorph Dataset 1 (pdb code 6gb8). 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: Small Cell Polymorph Dataset 1, PDB code: 6gb8:
Jump to Copper binding site number: 1; 2;

Copper binding site 1 out of 2 in the Copper Nitrite Reductase From Achromobacter Cycloclastes: Small Cell Polymorph 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: Small Cell Polymorph Dataset 1 within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu501 b:21.1 occ:1.00 ND1 A:HIS145 2.0 18.5 1.0 ND1 A:HIS95 2.1 18.0 1.0 SG A:CYS136 2.2 18.2 1.0 SD A:MET150 2.6 19.6 1.0 CE1 A:HIS145 2.9 18.8 1.0 CE1 A:HIS95 3.0 17.8 1.0 CG A:HIS145 3.1 18.6 1.0 CG A:HIS95 3.1 18.0 1.0 CB A:CYS136 3.3 17.1 1.0 CE A:MET150 3.3 20.8 1.0 CB A:HIS95 3.5 18.0 1.0 CB A:HIS145 3.5 17.8 1.0 CA A:HIS95 3.8 18.8 1.0 NE2 A:HIS145 4.0 19.4 1.0 CG A:MET150 4.1 18.9 1.0 CD2 A:HIS145 4.1 19.1 1.0 NE2 A:HIS95 4.2 17.6 1.0 CG A:PRO138 4.2 21.7 1.0 CD2 A:HIS95 4.2 18.2 1.0 O A:LEU94 4.2 20.3 1.0 CB A:MET150 4.5 17.4 1.0 SD A:MET62 4.5 20.9 1.0 N A:ASN96 4.6 18.9 1.0 CD A:PRO138 4.7 21.2 1.0 CA A:CYS136 4.7 16.6 1.0 CA A:HIS145 4.8 17.2 1.0 C A:HIS95 4.8 19.0 1.0 N A:HIS95 4.8 19.9 1.0 C A:LEU94 4.9 22.6 1.0 CB A:MET62 5.0 19.5 1.0

Copper binding site 2 out of 2 in the Copper Nitrite Reductase From Achromobacter Cycloclastes: Small Cell Polymorph 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: Small Cell Polymorph Dataset 1 within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu502 b:17.1 occ:1.00 NE2 A:HIS100 2.0 13.8 1.0 NE2 A:HIS135 2.1 16.0 1.0 O2 A:NO2503 2.1 25.6 1.0 O1 A:NO2503 2.2 21.0 1.0 N A:NO2503 2.2 26.6 1.0 CE1 A:HIS100 3.0 15.1 1.0 CD2 A:HIS135 3.0 16.8 1.0 CD2 A:HIS100 3.1 13.9 1.0 CE1 A:HIS135 3.1 16.3 1.0 OD2 A:ASP98 4.0 28.4 1.0 ND1 A:HIS100 4.1 14.5 1.0 CG A:HIS135 4.2 16.6 1.0 ND1 A:HIS135 4.2 16.6 1.0 CG A:HIS100 4.2 14.3 1.0 CG A:ASP98 4.6 23.8 1.0 OD1 A:ASP98 4.8 22.2 1.0 O A:HOH713 4.9 20.2 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