Copper in PDB 1w2z: Psao and Xenon

All present enzymatic activity of Psao and Xenon:
1.4.3.6;

The structure of Psao and Xenon, PDB code: 1w2z was solved by A.P.Duff, D.M.Trambaiolo, A.E.Cohen, P.J.Ellis, G.A.Juda, E.M.Shepard, D.B.Langley, D.M.Dooley, H.C.Freeman, J.M.Guss, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	29.88 / 2.24
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	89.507, 196.268, 89.665, 90.00, 107.46, 90.00
R / Rfree (%)	17.9 / 22.4

The structure of Psao and Xenon also contains other interesting chemical elements:

Manganese	(Mn)	4 atoms
Xenon	(Xe)	8 atoms
Iodine	(I)	176 atoms

The binding sites of Copper atom in the Psao and Xenon (pdb code 1w2z). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total 4 binding sites of Copper where determined in the Psao and Xenon, PDB code: 1w2z:
Jump to Copper binding site number: 1; 2; 3; 4;

Copper binding site 1 out of 4 in the Psao and Xenon


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of Psao and Xenon within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu701 b:34.1 occ:1.00 NE2 A:HIS442 2.1 8.4 1.0 NE2 A:HIS444 2.2 12.7 1.0 ND1 A:HIS603 2.2 10.8 1.0 O A:HOH2106 2.9 33.0 1.0 CD2 A:HIS442 2.9 10.7 1.0 CD2 A:HIS444 3.0 13.7 1.0 HD2 A:HIS444 3.0 13.3 1.0 HB2 A:HIS603 3.0 14.6 1.0 HD2 A:HIS442 3.1 10.0 1.0 CE1 A:HIS442 3.1 11.6 1.0 CG A:HIS603 3.1 14.1 1.0 CE1 A:HIS603 3.2 12.1 1.0 HB3 A:HIS603 3.3 14.6 1.0 CE1 A:HIS444 3.3 17.9 1.0 CB A:HIS603 3.3 14.8 1.0 HE1 A:HIS442 3.3 10.6 1.0 HE1 A:HIS603 3.4 13.7 1.0 HE1 A:HIS444 3.6 13.1 1.0 HD12 A:LEU407 3.6 33.7 1.0 CG A:HIS442 4.1 10.8 1.0 ND1 A:HIS442 4.1 10.3 1.0 HD13 A:ILE601 4.2 24.2 1.0 CG A:HIS444 4.2 13.7 1.0 CD2 A:HIS603 4.3 18.1 1.0 NE2 A:HIS603 4.3 16.3 1.0 ND1 A:HIS444 4.3 9.4 1.0 HE3 A:MET613 4.4 21.9 0.6 O2 A:TPQ387 4.5 26.6 0.4 CD1 A:LEU407 4.5 35.2 1.0 HD12 A:ILE601 4.6 24.2 1.0 HD11 A:LEU407 4.7 33.7 1.0 HD13 A:LEU407 4.8 33.7 1.0 HD22 A:LEU411 4.8 13.4 1.0 CA A:HIS603 4.8 14.6 1.0 CD1 A:ILE601 4.8 25.5 1.0 HE2 A:MET613 4.9 29.0 0.4 H3 A:TPQ387 4.9 27.6 0.4

Copper binding site 2 out of 4 in the Psao and Xenon


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 2 of Psao and Xenon within 5.0Å range: probe atom residue distance (Å) B Occ B:Cu701 b:31.4 occ:1.00 ND1 B:HIS603 2.0 12.6 1.0 NE2 B:HIS442 2.1 10.8 1.0 NE2 B:HIS444 2.1 11.1 1.0 O B:HOH2086 2.8 32.2 1.0 CD2 B:HIS442 2.9 10.5 1.0 CG B:HIS603 3.0 16.0 1.0 CE1 B:HIS603 3.0 13.1 1.0 HB2 B:HIS603 3.0 14.7 1.0 CD2 B:HIS444 3.1 15.7 1.0 CE1 B:HIS442 3.1 12.6 1.0 HD2 B:HIS442 3.1 10.1 1.0 CE1 B:HIS444 3.1 14.8 1.0 HE1 B:HIS603 3.2 13.7 1.0 HD2 B:HIS444 3.2 13.3 1.0 HB3 B:HIS603 3.2 14.7 1.0 CB B:HIS603 3.3 15.4 1.0 HE1 B:HIS444 3.3 12.9 1.0 HE1 B:HIS442 3.3 10.8 1.0 HD12 B:LEU407 3.5 33.9 1.0 CG B:HIS442 4.1 12.5 1.0 ND1 B:HIS442 4.1 10.5 1.0 NE2 B:HIS603 4.1 13.0 1.0 CD2 B:HIS603 4.1 16.3 1.0 ND1 B:HIS444 4.2 11.2 1.0 CG B:HIS444 4.2 12.3 1.0 HD13 B:ILE601 4.3 24.2 1.0 HE2 B:MET613 4.3 21.9 0.6 CD1 B:LEU407 4.4 36.2 1.0 HD23 B:LEU407 4.5 33.0 1.0 HD21 B:LEU407 4.6 33.0 1.0 H3 B:TPQ387 4.6 27.6 0.4 O2 B:TPQ387 4.6 26.3 0.4 HD12 B:ILE601 4.6 24.2 1.0 HD11 B:LEU407 4.7 33.9 1.0 HD13 B:LEU407 4.7 33.9 1.0 CA B:HIS603 4.8 14.6 1.0 HE2 B:MET613 4.9 29.0 0.4 CD1 B:ILE601 4.9 23.9 1.0 HD22 B:LEU411 4.9 13.3 1.0 CD2 B:LEU407 4.9 34.2 1.0 HD2 B:HIS603 5.0 15.5 1.0

Copper binding site 3 out of 4 in the Psao and Xenon


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 3 of Psao and Xenon within 5.0Å range: probe atom residue distance (Å) B Occ C:Cu701 b:33.7 occ:1.00 NE2 C:HIS444 2.1 12.6 1.0 NE2 C:HIS442 2.1 8.7 1.0 ND1 C:HIS603 2.1 12.0 1.0 O C:HOH2059 2.9 39.3 1.0 CD2 C:HIS442 2.9 10.3 1.0 HB2 C:HIS603 3.0 14.6 1.0 CE1 C:HIS444 3.0 11.3 1.0 CG C:HIS603 3.0 16.1 1.0 HD2 C:HIS442 3.1 9.9 1.0 CE1 C:HIS442 3.1 8.4 1.0 CE1 C:HIS603 3.1 16.4 1.0 CD2 C:HIS444 3.1 13.0 1.0 HE1 C:HIS444 3.2 12.6 1.0 HB3 C:HIS603 3.3 14.6 1.0 HE1 C:HIS603 3.3 13.9 1.0 HD2 C:HIS444 3.3 13.2 1.0 CB C:HIS603 3.3 14.0 1.0 HE1 C:HIS442 3.4 10.4 1.0 HD12 C:LEU407 3.7 33.7 1.0 CG C:HIS442 4.1 10.4 1.0 ND1 C:HIS442 4.1 11.1 1.0 ND1 C:HIS444 4.2 7.5 1.0 CD2 C:HIS603 4.2 15.5 1.0 NE2 C:HIS603 4.2 13.0 1.0 CG C:HIS444 4.2 14.3 1.0 HD13 C:ILE601 4.3 24.3 1.0 O2 C:TPQ387 4.3 27.0 0.4 HD12 C:ILE601 4.4 24.3 1.0 HE3 C:MET613 4.4 21.8 0.6 CD1 C:LEU407 4.5 35.0 1.0 HD11 C:LEU407 4.7 33.7 1.0 HE2 C:MET613 4.8 29.1 0.4 CD1 C:ILE601 4.8 25.6 1.0 HD13 C:LEU407 4.8 33.7 1.0 CA C:HIS603 4.8 14.4 1.0 HD22 C:LEU411 4.8 13.3 1.0 H3 C:TPQ387 5.0 27.7 0.4

Copper binding site 4 out of 4 in the Psao and Xenon


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 4 of Psao and Xenon within 5.0Å range: probe atom residue distance (Å) B Occ D:Cu701 b:29.5 occ:1.00 NE2 D:HIS444 2.0 10.2 1.0 ND1 D:HIS603 2.0 11.6 1.0 NE2 D:HIS442 2.1 8.4 1.0 O D:HOH2083 2.8 36.9 1.0 CD2 D:HIS442 3.0 9.1 1.0 CG D:HIS603 3.0 14.6 1.0 HB2 D:HIS603 3.0 14.6 1.0 CE1 D:HIS444 3.0 15.0 1.0 CD2 D:HIS444 3.0 13.7 1.0 CE1 D:HIS603 3.1 16.7 1.0 CE1 D:HIS442 3.1 13.6 1.0 HD2 D:HIS442 3.1 9.8 1.0 HB3 D:HIS603 3.2 14.6 1.0 HE1 D:HIS444 3.2 12.9 1.0 HD2 D:HIS444 3.2 13.2 1.0 CB D:HIS603 3.3 14.5 1.0 HE1 D:HIS603 3.3 14.0 1.0 HE1 D:HIS442 3.3 10.7 1.0 HD12 D:LEU407 3.7 33.8 1.0 CG D:HIS442 4.1 8.5 1.0 ND1 D:HIS442 4.1 9.6 1.0 ND1 D:HIS444 4.1 11.8 1.0 CD2 D:HIS603 4.1 14.8 1.0 NE2 D:HIS603 4.1 14.4 1.0 CG D:HIS444 4.2 11.8 1.0 HE3 D:MET613 4.3 21.9 0.6 HD13 D:ILE601 4.4 24.2 1.0 CD1 D:LEU407 4.5 36.0 1.0 HD12 D:ILE601 4.6 24.2 1.0 HD11 D:LEU407 4.6 33.8 1.0 O2 D:TPQ387 4.7 27.9 0.4 HD13 D:LEU407 4.8 33.8 1.0 CA D:HIS603 4.8 14.4 1.0 HD22 D:LEU411 4.8 13.3 1.0 CD1 D:ILE601 4.9 25.5 1.0 HD2 D:HIS603 5.0 15.4 1.0

A.P.Duff, D.M.Trambaiolo, A.E.Cohen, P.J.Ellis, G.A.Juda, E.M.Shepard, D.B.Langley, D.M.Dooley, H.C.Freeman, J.M.Guss. Using Xenon As A Probe For Dioxygen-Binding Sites in Copper Amine Oxidases. J.Mol.Biol. V. 344 599 2004.
ISSN: ISSN 0022-2836
PubMed: 15533431
DOI: 10.1016/J.JMB.2004.09.075