Copper in PDB 5n8h: Serial Cu Nitrite Reductase Structures at Elevated Cryogenic Temperature, 240K. Dataset 3.

All present enzymatic activity of Serial Cu Nitrite Reductase Structures at Elevated Cryogenic Temperature, 240K. Dataset 3.:
1.7.2.1;

The structure of Serial Cu Nitrite Reductase Structures at Elevated Cryogenic Temperature, 240K. Dataset 3., PDB code: 5n8h was solved by S.Horrell, D.Kekilli, M.Hough, R.Strange, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	29.00 / 1.65
Space group	P 21 3
Cell size a, b, c (Å), α, β, γ (°)	96.204, 96.204, 96.204, 90.00, 90.00, 90.00
R / Rfree (%)	14.4 / 17

The binding sites of Copper atom in the Serial Cu Nitrite Reductase Structures at Elevated Cryogenic Temperature, 240K. Dataset 3. (pdb code 5n8h). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total 2 binding sites of Copper where determined in the Serial Cu Nitrite Reductase Structures at Elevated Cryogenic Temperature, 240K. Dataset 3., PDB code: 5n8h:
Jump to Copper binding site number: 1; 2;

Copper binding site 1 out of 2 in the Serial Cu Nitrite Reductase Structures at Elevated Cryogenic Temperature, 240K. Dataset 3.


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of Serial Cu Nitrite Reductase Structures at Elevated Cryogenic Temperature, 240K. Dataset 3. within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu501 b:18.8 occ:1.00 ND1 A:HIS95 2.1 16.2 1.0 ND1 A:HIS145 2.1 17.8 1.0 SG A:CYS136 2.2 14.2 1.0 SD A:MET150 2.5 18.3 1.0 CE1 A:HIS145 3.0 17.2 1.0 CE1 A:HIS95 3.0 16.9 1.0 CG A:HIS95 3.1 15.7 1.0 CB A:CYS136 3.2 12.3 1.0 CE A:MET150 3.3 19.2 1.0 CG A:HIS145 3.3 15.8 1.0 CB A:HIS95 3.4 14.7 1.0 CB A:HIS145 3.7 14.3 1.0 CA A:HIS95 3.8 14.7 1.0 CG A:MET150 4.0 16.4 1.0 NE2 A:HIS95 4.1 16.4 1.0 NE2 A:HIS145 4.2 17.0 1.0 CD2 A:HIS95 4.2 15.6 1.0 O A:LEU94 4.3 17.9 1.0 CD2 A:HIS145 4.3 16.2 1.0 CG A:PRO138 4.4 18.8 1.0 CB A:MET150 4.4 13.6 1.0 SD A:MET62 4.6 19.8 1.0 N A:ASN96 4.6 13.7 1.0 CA A:CYS136 4.6 12.1 1.0 CD A:PRO138 4.8 17.9 1.0 C A:HIS95 4.8 14.7 1.0 N A:HIS95 4.8 15.9 1.0 CA A:HIS145 4.9 13.6 1.0 C A:LEU94 5.0 18.4 1.0

Copper binding site 2 out of 2 in the Serial Cu Nitrite Reductase Structures at Elevated Cryogenic Temperature, 240K. Dataset 3.


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 2 of Serial Cu Nitrite Reductase Structures at Elevated Cryogenic Temperature, 240K. Dataset 3. within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu502 b:13.0 occ:1.00 NE2 A:HIS135 2.0 11.3 1.0 NE2 A:HIS100 2.1 10.4 1.0 O A:HOH832 2.2 36.7 1.0 CE1 A:HIS100 2.9 9.9 1.0 CD2 A:HIS135 3.0 10.7 1.0 CE1 A:HIS135 3.1 11.3 1.0 CD2 A:HIS100 3.1 10.1 1.0 OD2 A:ASP98 4.0 20.0 1.0 ND1 A:HIS100 4.1 9.9 1.0 ND1 A:HIS135 4.2 10.8 1.0 CG A:HIS135 4.2 10.1 1.0 CG A:HIS100 4.2 9.6 1.0 CG A:ASP98 4.5 16.7 1.0 OD1 A:ASP98 4.7 15.7 1.0

K.Sen, S.Horrell, D.Kekilli, C.W.Yong, T.W.Keal, H.Atakisi, D.W.Moreau, R.E.Thorne, M.A.Hough, R.W.Strange. Active-Site Protein Dynamics and Solvent Accessibility in Native Achromobacter Cycloclastes Copper Nitrite Reductase. Iucrj V. 4 495 2017.
ISSN: ESSN 2052-2525
PubMed: 28875036
DOI: 10.1107/S2052252517007527