Copper in PDB 5og5: Cu Nitrite Reductase Serial Data at Varying Temperatures Rt 0.21MGY

All present enzymatic activity of Cu Nitrite Reductase Serial Data at Varying Temperatures Rt 0.21MGY:
1.7.2.1;

The structure of Cu Nitrite Reductase Serial Data at Varying Temperatures Rt 0.21MGY, PDB code: 5og5 was solved by S.Horrell, D.Kekilli, R.W.Strange, M.A.Hough, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	48.13 / 1.82
Space group	P 21 3
Cell size a, b, c (Å), α, β, γ (°)	96.252, 96.252, 96.252, 90.00, 90.00, 90.00
R / Rfree (%)	17.4 / 20.9

The binding sites of Copper atom in the Cu Nitrite Reductase Serial Data at Varying Temperatures Rt 0.21MGY (pdb code 5og5). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total 2 binding sites of Copper where determined in the Cu Nitrite Reductase Serial Data at Varying Temperatures Rt 0.21MGY, PDB code: 5og5:
Jump to Copper binding site number: 1; 2;

Copper binding site 1 out of 2 in the Cu Nitrite Reductase Serial Data at Varying Temperatures Rt 0.21MGY


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of Cu Nitrite Reductase Serial Data at Varying Temperatures Rt 0.21MGY within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu501 b:19.3 occ:1.00 ND1 A:HIS145 2.0 18.0 1.0 ND1 A:HIS95 2.0 18.9 1.0 SG A:CYS136 2.3 16.8 1.0 SD A:MET150 2.4 17.6 1.0 CE1 A:HIS145 2.9 18.7 1.0 CE1 A:HIS95 2.9 18.0 1.0 CG A:HIS95 3.1 17.8 1.0 CG A:HIS145 3.1 16.9 1.0 CB A:CYS136 3.2 14.9 1.0 CE A:MET150 3.3 18.6 1.0 CB A:HIS95 3.5 18.2 1.0 CB A:HIS145 3.6 15.4 1.0 CA A:HIS95 3.9 18.1 1.0 CG A:MET150 3.9 17.5 1.0 NE2 A:HIS145 4.1 19.1 1.0 NE2 A:HIS95 4.1 17.4 1.0 CD2 A:HIS145 4.2 18.5 1.0 CD2 A:HIS95 4.2 18.2 1.0 O A:LEU94 4.3 18.9 1.0 CG A:PRO138 4.3 20.1 1.0 CB A:MET150 4.4 15.7 1.0 SD A:MET62 4.5 22.3 1.0 N A:ASN96 4.6 16.8 1.0 CA A:CYS136 4.7 14.9 1.0 CD A:PRO138 4.7 18.5 1.0 CA A:HIS145 4.8 15.1 1.0 C A:HIS95 4.8 17.8 1.0 N A:HIS95 4.8 18.4 1.0 C A:LEU94 5.0 20.7 1.0 CB A:MET62 5.0 20.6 1.0

Copper binding site 2 out of 2 in the Cu Nitrite Reductase Serial Data at Varying Temperatures Rt 0.21MGY


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 2 of Cu Nitrite Reductase Serial Data at Varying Temperatures Rt 0.21MGY within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu502 b:13.9 occ:1.00 NE2 A:HIS100 2.0 12.2 1.0 NE2 A:HIS135 2.1 13.2 1.0 O A:NO509 2.3 21.9 0.6 N A:NO509 2.3 23.8 0.6 CE1 A:HIS100 2.9 12.4 1.0 CD2 A:HIS135 3.1 13.5 1.0 CE1 A:HIS135 3.1 13.0 1.0 CD2 A:HIS100 3.1 12.5 1.0 OD2 A:ASP98 3.9 27.9 1.0 ND1 A:HIS100 4.1 12.7 1.0 ND1 A:HIS135 4.2 13.2 1.0 CG A:HIS100 4.2 12.1 1.0 CG A:HIS135 4.2 13.2 1.0 CG A:ASP98 4.5 20.3 1.0 OD1 A:ASP98 4.7 21.0 1.0 O A:HOH709 4.8 16.9 1.0

S.Horrell, D.Kekilli, K.Sen, R.L.Owen, F.S.N.Dworkowski, S.V.Antonyuk, T.W.Keal, C.W.Yong, R.R.Eady, S.S.Hasnain, R.W.Strange, M.A.Hough. Enzyme Catalysis Captured Using Multiple Structures From One Crystal at Varying Temperatures. Iucrj V. 5 283 2018.
ISSN: ESSN 2052-2525
PubMed: 29755744
DOI: 10.1107/S205225251800386X