Copper in PDB 4kff: Crystal Structure of Hansenula Polymorpha Copper Amine Oxidase-1 Reduced By Methylamine at pH 8.5

All present enzymatic activity of Crystal Structure of Hansenula Polymorpha Copper Amine Oxidase-1 Reduced By Methylamine at pH 8.5:
1.4.3.21;

The structure of Crystal Structure of Hansenula Polymorpha Copper Amine Oxidase-1 Reduced By Methylamine at pH 8.5, PDB code: 4kff was solved by B.J.Johnson, E.T.Yukl, 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)	38.56 / 2.15
Space group	C 2 2 21
Cell size a, b, c (Å), α, β, γ (°)	139.022, 153.316, 223.048, 90.00, 90.00, 90.00
R / Rfree (%)	14.2 / 18.5

The binding sites of Copper atom in the Crystal Structure of Hansenula Polymorpha Copper Amine Oxidase-1 Reduced By Methylamine at pH 8.5 (pdb code 4kff). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total 3 binding sites of Copper where determined in the Crystal Structure of Hansenula Polymorpha Copper Amine Oxidase-1 Reduced By Methylamine at pH 8.5, PDB code: 4kff:
Jump to Copper binding site number: 1; 2; 3;

Copper binding site 1 out of 3 in the Crystal Structure of Hansenula Polymorpha Copper Amine Oxidase-1 Reduced By Methylamine at pH 8.5


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of Crystal Structure of Hansenula Polymorpha Copper Amine Oxidase-1 Reduced By Methylamine at pH 8.5 within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu801 b:19.2 occ:1.00 ND1 A:HIS624 1.9 19.1 1.0 NE2 A:HIS458 2.0 15.8 1.0 NE2 A:HIS456 2.1 14.2 1.0 OH A:TYY405 2.8 16.6 0.7 CG A:HIS624 2.9 17.6 1.0 CE1 A:HIS624 2.9 19.2 1.0 CE1 A:HIS458 3.0 15.3 1.0 CD2 A:HIS458 3.0 13.7 1.0 CE1 A:HIS456 3.0 14.5 1.0 CD2 A:HIS456 3.0 14.4 1.0 CB A:HIS624 3.2 16.6 1.0 CZ A:TYY405 3.4 17.6 0.7 CD2 A:LEU425 3.8 37.9 1.0 CE1 A:TYY405 3.8 18.3 0.7 NE2 A:HIS624 4.0 19.7 1.0 CD2 A:HIS624 4.0 17.9 1.0 ND1 A:HIS458 4.1 15.0 1.0 CG A:HIS458 4.1 14.9 1.0 ND1 A:HIS456 4.1 15.1 1.0 CG A:HIS456 4.2 13.8 1.0 CE2 A:TYY405 4.4 18.9 0.7 O A:HOH983 4.5 15.1 1.0 OZ A:TYY405 4.5 18.2 0.3 CA A:HIS624 4.7 15.1 1.0 N5 A:TYY405 4.8 19.2 0.7 CD1 A:TYY405 4.9 20.4 0.7

Copper binding site 2 out of 3 in the Crystal Structure of Hansenula Polymorpha Copper Amine Oxidase-1 Reduced By Methylamine at pH 8.5


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 2 of Crystal Structure of Hansenula Polymorpha Copper Amine Oxidase-1 Reduced By Methylamine at pH 8.5 within 5.0Å range: probe atom residue distance (Å) B Occ B:Cu801 b:18.2 occ:1.00 NE2 B:HIS458 2.0 14.1 1.0 ND1 B:HIS624 2.0 16.6 1.0 NE2 B:HIS456 2.2 14.0 1.0 OH B:TYY405 2.9 18.2 0.7 CD2 B:HIS458 3.0 12.9 1.0 CG B:HIS624 3.0 15.2 1.0 CE1 B:HIS458 3.0 14.1 1.0 CE1 B:HIS624 3.0 16.0 1.0 CD2 B:HIS456 3.0 13.7 1.0 CE1 B:HIS456 3.2 15.1 1.0 CB B:HIS624 3.3 16.3 1.0 CZ B:TYY405 3.5 17.2 0.7 CD2 B:LEU425 3.8 35.7 1.0 CE1 B:TYY405 4.0 17.8 0.7 ND1 B:HIS458 4.1 13.8 1.0 NE2 B:HIS624 4.1 16.4 1.0 CG B:HIS458 4.1 13.8 1.0 CD2 B:HIS624 4.1 14.8 1.0 CG B:HIS456 4.2 14.6 1.0 ND1 B:HIS456 4.3 14.8 1.0 CE2 B:TYY405 4.4 20.3 0.7 OZ B:TYY405 4.5 18.1 0.3 O B:HOH921 4.5 13.7 1.0 N5 B:TYY405 4.7 18.2 0.7 CA B:HIS624 4.8 15.0 1.0 CD1 B:ILE622 5.0 23.0 1.0

Copper binding site 3 out of 3 in the Crystal Structure of Hansenula Polymorpha Copper Amine Oxidase-1 Reduced By Methylamine at pH 8.5


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 3 of Crystal Structure of Hansenula Polymorpha Copper Amine Oxidase-1 Reduced By Methylamine at pH 8.5 within 5.0Å range: probe atom residue distance (Å) B Occ C:Cu702 b:18.7 occ:1.00 ND1 C:HIS624 2.0 16.2 1.0 NE2 C:HIS458 2.1 18.4 1.0 NE2 C:HIS456 2.1 16.0 1.0 OH C:TYY405 2.9 12.5 0.7 CD2 C:HIS456 3.0 15.3 1.0 CG C:HIS624 3.0 14.9 1.0 CD2 C:HIS458 3.0 18.2 1.0 CE1 C:HIS624 3.0 17.2 1.0 CE1 C:HIS458 3.1 19.5 1.0 CE1 C:HIS456 3.1 15.6 1.0 CB C:HIS624 3.3 14.4 1.0 CZ C:TYY405 3.5 14.2 0.7 CD2 C:LEU425 3.7 34.2 1.0 CE1 C:TYY405 4.0 14.6 0.7 CD2 C:HIS624 4.1 15.5 1.0 NE2 C:HIS624 4.1 16.4 1.0 CG C:HIS456 4.1 15.3 1.0 CG C:HIS458 4.1 18.6 1.0 ND1 C:HIS458 4.2 19.9 1.0 ND1 C:HIS456 4.2 15.2 1.0 OZ C:TYY405 4.4 18.1 0.3 CE2 C:TYY405 4.4 15.7 0.7 O C:HOH831 4.5 13.3 1.0 CA C:HIS624 4.8 14.4 1.0 N5 C:TYY405 4.8 17.1 0.7

B.J.Johnson, E.T.Yukl, V.J.Klema, J.P.Klinman, C.M.Wilmot. Structural Evidence For the Semiquinone in A Copper Amine Oxidase From Hansenula Polymorpha: Implications For the Catalytic Mechanism J.Biol.Chem. 2013.
ISSN: ESSN 1083-351X