Copper in PDB 3t0u: Hansenula Polymorpha Copper Amine Oxidase-1 in Complex with Cu(I)

All present enzymatic activity of Hansenula Polymorpha Copper Amine Oxidase-1 in Complex with Cu(I):
1.4.3.21;

The structure of Hansenula Polymorpha Copper Amine Oxidase-1 in Complex with Cu(I), PDB code: 3t0u was solved by V.J.Klema, C.M.Wilmot, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	49.14 / 1.90
Space group	C 2 2 21
Cell size a, b, c (Å), α, β, γ (°)	139.447, 153.673, 223.476, 90.00, 90.00, 90.00
R / Rfree (%)	12.5 / 16.8

The binding sites of Copper atom in the Hansenula Polymorpha Copper Amine Oxidase-1 in Complex with Cu(I) (pdb code 3t0u). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total 3 binding sites of Copper where determined in the Hansenula Polymorpha Copper Amine Oxidase-1 in Complex with Cu(I), PDB code: 3t0u:
Jump to Copper binding site number: 1; 2; 3;

Copper binding site 1 out of 3 in the Hansenula Polymorpha Copper Amine Oxidase-1 in Complex with Cu(I)


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of Hansenula Polymorpha Copper Amine Oxidase-1 in Complex with Cu(I) within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu801 b:9.6 occ:1.00 NE2 A:HIS458 2.0 5.6 1.0 ND1 A:HIS624 2.1 9.2 1.0 NE2 A:HIS456 2.1 4.9 1.0 OH A:TYR405 2.8 10.5 1.0 CD2 A:HIS458 3.0 6.3 1.0 CD2 A:HIS456 3.0 3.8 1.0 CG A:HIS624 3.0 6.3 1.0 CE1 A:HIS458 3.0 4.7 1.0 CE1 A:HIS624 3.1 8.5 1.0 CE1 A:HIS456 3.1 5.0 1.0 CB A:HIS624 3.2 6.7 1.0 CZ A:TYR405 3.5 13.0 1.0 CD2 A:LEU425 3.6 8.4 0.5 CE2 A:TYR405 4.0 15.8 1.0 ND1 A:HIS458 4.1 6.1 1.0 CG A:HIS458 4.1 5.7 1.0 CG A:HIS456 4.1 5.4 1.0 CD2 A:HIS624 4.1 5.9 1.0 CE1 A:TYR405 4.2 18.1 1.0 ND1 A:HIS456 4.2 4.9 1.0 NE2 A:HIS624 4.2 6.6 1.0 O A:HOH1238 4.6 6.0 1.0 CA A:HIS624 4.8 5.3 1.0 CD1 A:ILE622 4.8 16.4 1.0 CD1 A:LEU425 4.8 10.6 0.5 CG A:LEU425 5.0 8.2 0.5

Copper binding site 2 out of 3 in the Hansenula Polymorpha Copper Amine Oxidase-1 in Complex with Cu(I)


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 2 of Hansenula Polymorpha Copper Amine Oxidase-1 in Complex with Cu(I) within 5.0Å range: probe atom residue distance (Å) B Occ B:Cu801 b:9.4 occ:1.00 ND1 B:HIS624 2.0 8.2 1.0 NE2 B:HIS458 2.0 5.8 1.0 NE2 B:HIS456 2.1 6.2 1.0 OH B:TYR405 2.8 10.0 1.0 CG B:HIS624 2.9 7.5 1.0 CD2 B:HIS458 2.9 7.4 1.0 CE1 B:HIS624 3.0 10.5 1.0 CE1 B:HIS458 3.0 6.9 1.0 CD2 B:HIS456 3.0 7.5 1.0 CE1 B:HIS456 3.1 3.5 1.0 CB B:HIS624 3.2 5.1 1.0 CZ B:TYR405 3.5 13.9 1.0 CD2 B:LEU425 3.7 17.3 0.6 CE2 B:TYR405 4.0 14.4 1.0 CD2 B:HIS624 4.1 5.5 1.0 NE2 B:HIS624 4.1 8.7 1.0 ND1 B:HIS458 4.1 8.0 1.0 CG B:HIS458 4.1 6.3 1.0 CG B:HIS456 4.2 4.0 1.0 ND1 B:HIS456 4.2 7.5 1.0 CE1 B:TYR405 4.3 21.0 1.0 O B:HOH1116 4.6 8.5 1.0 CA B:HIS624 4.8 4.6 1.0 CD1 B:LEU425 4.9 8.3 0.4 CD1 B:ILE622 5.0 12.8 1.0 CG B:LEU425 5.0 13.0 0.6

Copper binding site 3 out of 3 in the Hansenula Polymorpha Copper Amine Oxidase-1 in Complex with Cu(I)


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 3 of Hansenula Polymorpha Copper Amine Oxidase-1 in Complex with Cu(I) within 5.0Å range: probe atom residue distance (Å) B Occ C:Cu801 b:9.0 occ:1.00 ND1 C:HIS624 2.0 9.2 1.0 NE2 C:HIS458 2.0 7.0 1.0 NE2 C:HIS456 2.1 6.3 1.0 OH C:TYR405 2.8 14.5 1.0 CG C:HIS624 2.9 7.7 1.0 CD2 C:HIS458 2.9 3.7 1.0 CD2 C:HIS456 3.0 8.6 1.0 CE1 C:HIS456 3.0 9.0 1.0 CE1 C:HIS624 3.1 8.7 1.0 CE1 C:HIS458 3.1 5.8 1.0 CB C:HIS624 3.2 4.9 1.0 CZ C:TYR405 3.4 12.8 1.0 CD2 C:LEU425 3.7 11.0 0.5 CE2 C:TYR405 4.0 14.1 1.0 CD2 C:HIS624 4.1 7.6 1.0 CG C:HIS458 4.1 3.8 1.0 ND1 C:HIS456 4.1 5.8 1.0 CG C:HIS456 4.1 4.8 1.0 NE2 C:HIS624 4.1 9.0 1.0 ND1 C:HIS458 4.1 6.3 1.0 CE1 C:TYR405 4.3 15.4 1.0 O C:HOH1153 4.6 9.0 1.0 CA C:HIS624 4.7 5.8 1.0 CD1 C:ILE622 4.9 19.5 1.0 CG C:LEU425 5.0 7.7 0.5

V.J.Klema, B.J.Johnson, J.P.Klinman, C.M.Wilmot. The Precursor Form of Hansenula Polymorpha Copper Amine Oxidase 1 in Complex with Cui and Coii. Acta Crystallogr.,Sect.F V. 68 501 2012.
ISSN: ESSN 1744-3091
PubMed: 22691777
DOI: 10.1107/S1744309112012857