Copper in PDB 1spu: Structure of Oxidoreductase

All present enzymatic activity of Structure of Oxidoreductase:
1.4.3.6;

The structure of Structure of Oxidoreductase, PDB code: 1spu was solved by C.M.Wilmot, S.E.V.Phillips, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	20.00 / 2.00
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	134.460, 166.070, 79.410, 90.00, 90.00, 90.00
R / Rfree (%)	20.6 / n/a

The binding sites of Copper atom in the Structure of Oxidoreductase (pdb code 1spu). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total 2 binding sites of Copper where determined in the Structure of Oxidoreductase, PDB code: 1spu:
Jump to Copper binding site number: 1; 2;

Copper binding site 1 out of 2 in the Structure of Oxidoreductase


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of Structure of Oxidoreductase within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu800 b:25.2 occ:1.00 NE2 A:HIS526 2.1 17.7 1.0 ND1 A:HIS689 2.3 13.6 1.0 NE2 A:HIS524 2.4 27.8 1.0 O A:HOH1277 2.4 22.9 1.0 O A:HOH1422 2.9 52.2 1.0 CD2 A:HIS526 2.9 21.0 1.0 CD2 A:HIS524 3.1 17.1 1.0 CG A:HIS689 3.2 19.4 1.0 CE1 A:HIS526 3.2 18.4 1.0 CE1 A:HIS524 3.3 20.8 1.0 CE1 A:HIS689 3.3 23.8 1.0 CB A:HIS689 3.3 14.6 1.0 O A:HOH1057 4.1 24.4 1.0 CG A:HIS526 4.1 15.1 1.0 CG A:HIS524 4.2 24.0 1.0 ND1 A:HIS526 4.3 18.8 1.0 ND1 A:HIS524 4.3 19.1 1.0 CD2 A:HIS689 4.3 22.0 1.0 NE2 A:HIS689 4.4 22.2 1.0 SD A:MET699 4.6 58.5 1.0 O A:HOH1292 4.6 21.3 1.0 O2 A:PAQ466 4.7 20.3 1.0 CA A:HIS689 4.9 10.7 1.0

Copper binding site 2 out of 2 in the Structure of Oxidoreductase


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 2 of Structure of Oxidoreductase within 5.0Å range: probe atom residue distance (Å) B Occ B:Cu800 b:20.9 occ:1.00 NE2 B:HIS526 2.0 17.3 1.0 ND1 B:HIS689 2.3 13.3 1.0 NE2 B:HIS524 2.4 19.4 1.0 O B:HOH1443 2.7 16.1 1.0 O B:HOH1518 3.0 49.2 1.0 CD2 B:HIS526 3.0 14.9 1.0 CE1 B:HIS526 3.1 14.0 1.0 CD2 B:HIS524 3.1 8.0 1.0 CG B:HIS689 3.2 14.6 1.0 CE1 B:HIS689 3.4 15.0 1.0 CB B:HIS689 3.4 12.0 1.0 CE1 B:HIS524 3.5 13.8 1.0 ND1 B:HIS526 4.2 18.7 1.0 CG B:HIS526 4.2 11.5 1.0 O B:HOH1283 4.3 35.9 1.0 CG B:HIS524 4.3 13.7 1.0 CD2 B:HIS689 4.4 6.9 1.0 NE2 B:HIS689 4.4 18.7 1.0 ND1 B:HIS524 4.4 19.6 1.0 O B:HOH1214 4.6 14.5 1.0 CE B:MET699 4.7 21.6 1.0 O2 B:PAQ466 4.7 22.6 1.0 SD B:MET699 4.7 34.3 1.0 O B:HOH1508 4.7 28.1 1.0 CE1 B:HIS613 4.8 15.8 1.0 CA B:HIS689 4.9 16.2 1.0 O B:HOH1442 5.0 22.1 1.0

C.M.Wilmot, J.M.Murray, G.Alton, M.R.Parsons, M.A.Convery, V.Blakeley, A.S.Corner, M.M.Palcic, P.F.Knowles, M.J.Mcpherson, S.E.Phillips. Catalytic Mechanism of the Quinoenzyme Amine Oxidase From Escherichia Coli: Exploring the Reductive Half-Reaction. Biochemistry V. 36 1608 1997.
ISSN: ISSN 0006-2960
PubMed: 9048544
DOI: 10.1021/BI962205J