Copper in PDB 6gti: Achromobacter Cycloclastes Copper Nitrite Reductase at pH 5.0

All present enzymatic activity of Achromobacter Cycloclastes Copper Nitrite Reductase at pH 5.0:
1.7.2.1;

The structure of Achromobacter Cycloclastes Copper Nitrite Reductase at pH 5.0, PDB code: 6gti was solved by T.P.Halsted, R.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)	7.90 / 1.50
Space group	P 21 3
Cell size a, b, c (Å), α, β, γ (°)	95.422, 95.422, 95.422, 90.00, 90.00, 90.00
R / Rfree (%)	15.3 / 17.8

The binding sites of Copper atom in the Achromobacter Cycloclastes Copper Nitrite Reductase at pH 5.0 (pdb code 6gti). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total 2 binding sites of Copper where determined in the Achromobacter Cycloclastes Copper Nitrite Reductase at pH 5.0, PDB code: 6gti:
Jump to Copper binding site number: 1; 2;

Copper binding site 1 out of 2 in the Achromobacter Cycloclastes Copper Nitrite Reductase at pH 5.0


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of Achromobacter Cycloclastes Copper Nitrite Reductase at pH 5.0 within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu501 b:11.3 occ:1.00 ND1 A:HIS145 2.0 10.4 1.0 ND1 A:HIS95 2.0 9.4 1.0 SG A:CYS136 2.2 10.9 1.0 SD A:MET150 2.5 11.3 1.0 CE1 A:HIS145 2.9 10.5 1.0 CE1 A:HIS95 3.0 10.1 1.0 CG A:HIS95 3.0 10.6 1.0 CG A:HIS145 3.1 10.1 1.0 CB A:CYS136 3.3 9.7 1.0 CE A:MET150 3.3 10.0 1.0 CB A:HIS95 3.4 10.8 1.0 CB A:HIS145 3.5 9.9 1.0 CG A:MET150 3.8 9.7 1.0 CA A:HIS95 3.9 11.0 1.0 NE2 A:HIS145 4.0 11.1 1.0 NE2 A:HIS95 4.1 11.4 1.0 CD2 A:HIS145 4.1 11.6 1.0 CD2 A:HIS95 4.1 10.4 1.0 O A:LEU94 4.3 13.3 1.0 CG A:PRO138 4.3 11.8 1.0 CB A:MET150 4.3 9.7 1.0 SD A:MET62 4.4 13.0 1.0 N A:ASN96 4.7 10.8 1.0 CA A:CYS136 4.7 9.9 1.0 CA A:HIS145 4.7 9.4 1.0 CD A:PRO138 4.8 11.7 1.0 C A:HIS95 4.9 11.6 1.0 N A:HIS95 4.9 11.4 1.0 CB A:MET62 4.9 11.3 1.0 C A:LEU94 5.0 12.5 1.0

Copper binding site 2 out of 2 in the Achromobacter Cycloclastes Copper Nitrite Reductase at pH 5.0


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 2 of Achromobacter Cycloclastes Copper Nitrite Reductase at pH 5.0 within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu502 b:10.5 occ:1.00 O2 A:NO2503 2.0 11.2 0.5 O2 A:NO2503 2.0 10.9 0.5 NE2 A:HIS100 2.0 10.4 1.0 NE2 A:HIS135 2.1 9.0 1.0 O1 A:NO2503 2.1 12.9 0.5 O1 A:NO2503 2.2 12.8 0.5 N A:NO2503 2.3 13.5 0.5 N A:NO2503 2.4 12.3 0.5 CE1 A:HIS100 3.0 10.4 1.0 CD2 A:HIS135 3.0 10.2 1.0 CE1 A:HIS135 3.1 10.1 1.0 CD2 A:HIS100 3.1 10.1 1.0 OD2 A:ASP98 3.8 9.2 0.5 ND1 A:HIS100 4.1 9.1 1.0 ND1 A:HIS135 4.2 10.1 1.0 CG A:HIS135 4.2 9.6 1.0 CG A:HIS100 4.2 8.8 1.0 O A:HOH615 4.4 14.9 0.5 CG A:ASP98 4.5 9.8 0.5 O A:HOH611 4.7 22.2 0.5 OD2 A:ASP98 4.8 14.6 0.5 OD1 A:ASP98 4.8 9.3 0.5 O A:HOH891 5.0 37.2 1.0

T.P.Halsted, K.Yamashita, C.C.Gopalasingam, R.T.Shenoy, K.Hirata, H.Ago, G.Ueno, M.P.Blakeley, R.R.Eady, S.V.Antonyuk, M.Yamamoto, S.S.Hasnain. Catalytically Important Damage-Free Structures of A Copper Nitrite Reductase Obtained By Femtosecond X-Ray Laser and Room-Temperature Neutron Crystallography. Iucrj V. 6 761 2019.
ISSN: ESSN 2052-2525
PubMed: 31316819
DOI: 10.1107/S2052252519008285