Copper in PDB 5n8i: Serial Cu Nitrite Reductase Structures at Elevated Cryogenic Temperature, 100K Reference Dataset.

All present enzymatic activity of Serial Cu Nitrite Reductase Structures at Elevated Cryogenic Temperature, 100K Reference Dataset.:
1.7.2.1;

The structure of Serial Cu Nitrite Reductase Structures at Elevated Cryogenic Temperature, 100K Reference Dataset., PDB code: 5n8i 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)	47.40 / 1.40
Space group	P 21 3
Cell size a, b, c (Å), α, β, γ (°)	94.793, 94.793, 94.793, 90.00, 90.00, 90.00
R / Rfree (%)	15.3 / 18.1

The binding sites of Copper atom in the Serial Cu Nitrite Reductase Structures at Elevated Cryogenic Temperature, 100K Reference Dataset. (pdb code 5n8i). 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, 100K Reference Dataset., PDB code: 5n8i:
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, 100K Reference Dataset.


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, 100K Reference Dataset. within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu501 b:9.8 occ:1.00 ND1 A:HIS145 2.0 10.1 1.0 ND1 A:HIS95 2.1 9.0 1.0 SG A:CYS136 2.2 9.8 1.0 SD A:MET150 2.5 9.1 1.0 CE1 A:HIS145 2.9 10.3 1.0 CE1 A:HIS95 3.0 9.1 1.0 CG A:HIS95 3.1 8.5 1.0 CG A:HIS145 3.1 9.7 1.0 CB A:CYS136 3.2 8.3 1.0 CE A:MET150 3.2 9.9 1.0 CB A:HIS95 3.5 8.9 1.0 CB A:HIS145 3.5 9.5 1.0 CA A:HIS95 3.8 9.6 1.0 CG A:MET150 3.9 8.1 1.0 NE2 A:HIS145 4.0 10.5 1.0 O A:LEU94 4.1 11.1 1.0 NE2 A:HIS95 4.1 9.7 1.0 CD2 A:HIS145 4.2 10.4 1.0 CD2 A:HIS95 4.2 9.0 1.0 CG A:PRO138 4.3 11.0 1.0 CB A:MET150 4.3 7.6 1.0 SD A:MET62 4.5 11.2 1.0 CD A:PRO138 4.6 10.7 1.0 CA A:CYS136 4.6 8.7 1.0 N A:ASN96 4.7 9.1 1.0 CA A:HIS145 4.7 8.8 1.0 N A:HIS95 4.8 9.2 1.0 C A:HIS95 4.9 9.8 1.0 CB A:MET62 4.9 10.6 1.0 C A:LEU94 4.9 10.8 1.0

Copper binding site 2 out of 2 in the Serial Cu Nitrite Reductase Structures at Elevated Cryogenic Temperature, 100K Reference Dataset.


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, 100K Reference Dataset. within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu502 b:10.0 occ:1.00 O A:HOH611 2.0 21.8 1.0 NE2 A:HIS100 2.0 8.6 1.0 NE2 A:HIS135 2.1 8.2 1.0 CE1 A:HIS100 3.0 8.4 1.0 CD2 A:HIS135 3.0 8.2 1.0 CE1 A:HIS135 3.1 8.7 1.0 CD2 A:HIS100 3.1 8.2 1.0 OD2 A:ASP98 3.9 16.9 1.0 O A:HOH744 4.1 32.8 1.0 ND1 A:HIS100 4.1 7.8 1.0 CG A:HIS135 4.2 8.3 1.0 ND1 A:HIS135 4.2 8.1 1.0 CG A:HIS100 4.2 8.0 1.0 CG A:ASP98 4.4 13.2 1.0 OD1 A:ASP98 4.6 14.5 1.0 O A:HOH847 4.9 16.2 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