Copper in PDB 6gt0: Nitrite-Bound Copper Nitrite Reductase From Achromobacter Cycloclastes Determined By Serial Femtosecond Rotation Crystallography

All present enzymatic activity of Nitrite-Bound Copper Nitrite Reductase From Achromobacter Cycloclastes Determined By Serial Femtosecond Rotation Crystallography:
1.7.2.1;

The structure of Nitrite-Bound Copper Nitrite Reductase From Achromobacter Cycloclastes Determined By Serial Femtosecond Rotation Crystallography, PDB code: 6gt0 was solved by T.P.Halsted, K.Yamashita, C.C.Gopalasingam, R.T.Shenoy, K.Hirata, H.Ago, G.Ueno, R.R.Eady, S.V.Antonyuk, M.Yamamoto, S.S.Hasnain, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	54.86 / 1.50
Space group	P 21 3
Cell size a, b, c (Å), α, β, γ (°)	94.920, 94.920, 94.920, 90.00, 90.00, 90.00
R / Rfree (%)	14.3 / 17.1

The binding sites of Copper atom in the Nitrite-Bound Copper Nitrite Reductase From Achromobacter Cycloclastes Determined By Serial Femtosecond Rotation Crystallography (pdb code 6gt0). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total 2 binding sites of Copper where determined in the Nitrite-Bound Copper Nitrite Reductase From Achromobacter Cycloclastes Determined By Serial Femtosecond Rotation Crystallography, PDB code: 6gt0:
Jump to Copper binding site number: 1; 2;

Copper binding site 1 out of 2 in the Nitrite-Bound Copper Nitrite Reductase From Achromobacter Cycloclastes Determined By Serial Femtosecond Rotation Crystallography


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of Nitrite-Bound Copper Nitrite Reductase From Achromobacter Cycloclastes Determined By Serial Femtosecond Rotation Crystallography within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu501 b:16.2 occ:1.00 ND1 A:HIS145 2.0 15.1 1.0 ND1 A:HIS95 2.0 15.9 1.0 SG A:CYS136 2.2 14.8 1.0 SD A:MET150 2.4 15.1 1.0 CE1 A:HIS145 2.9 14.9 1.0 CE1 A:HIS95 3.0 16.6 1.0 CG A:HIS95 3.0 15.3 1.0 CG A:HIS145 3.1 14.9 1.0 CB A:CYS136 3.2 14.0 1.0 CE A:MET150 3.3 14.5 1.0 CB A:HIS95 3.3 14.9 1.0 CB A:HIS145 3.5 14.6 1.0 CG A:MET150 3.8 14.4 1.0 CA A:HIS95 3.8 15.4 1.0 NE2 A:HIS145 4.1 15.8 1.0 NE2 A:HIS95 4.1 15.4 1.0 CD2 A:HIS145 4.1 15.3 1.0 CD2 A:HIS95 4.1 16.0 1.0 O A:LEU94 4.3 16.8 1.0 CB A:MET150 4.3 13.8 1.0 CG A:PRO138 4.3 16.9 1.0 SD A:MET62 4.4 16.6 1.0 CA A:CYS136 4.6 13.2 1.0 N A:ASN96 4.6 15.0 1.0 CA A:HIS145 4.6 15.1 1.0 CD A:PRO138 4.8 15.4 1.0 CB A:MET62 4.8 15.6 1.0 C A:HIS95 4.8 15.6 1.0 N A:HIS95 4.8 15.9 1.0 C A:LEU94 5.0 16.9 1.0

Copper binding site 2 out of 2 in the Nitrite-Bound Copper Nitrite Reductase From Achromobacter Cycloclastes Determined By Serial Femtosecond Rotation Crystallography


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 2 of Nitrite-Bound Copper Nitrite Reductase From Achromobacter Cycloclastes Determined By Serial Femtosecond Rotation Crystallography within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu502 b:16.2 occ:1.00 O2 A:NO2503 2.0 16.3 0.5 O2 A:NO2503 2.0 20.8 0.5 O1 A:NO2503 2.0 19.8 0.5 NE2 A:HIS100 2.0 15.4 1.0 O1 A:NO2503 2.0 15.3 0.5 NE2 A:HIS135 2.0 15.8 1.0 N A:NO2503 2.1 18.1 0.5 N A:NO2503 2.1 20.5 0.5 CE1 A:HIS100 3.0 14.4 1.0 CE1 A:HIS135 3.0 16.2 1.0 CD2 A:HIS100 3.1 15.2 1.0 CD2 A:HIS135 3.1 15.7 1.0 OD2 A:ASP98 3.8 14.8 0.5 ND1 A:HIS100 4.1 14.3 1.0 ND1 A:HIS135 4.2 15.5 1.0 CG A:HIS100 4.2 14.4 1.0 CG A:HIS135 4.2 14.7 1.0 O A:HOH615 4.3 23.3 0.5 CG A:ASP98 4.4 14.3 0.5 OD1 A:ASP98 4.8 13.8 0.5 OD2 A:ASP98 4.8 23.3 0.5

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