Copper in PDB 3loy: Crystal Structure of A Copper-Containing Benzylamine Oxidase From Hansenula Polymorpha

All present enzymatic activity of Crystal Structure of A Copper-Containing Benzylamine Oxidase From Hansenula Polymorpha:
1.4.3.21;

The structure of Crystal Structure of A Copper-Containing Benzylamine Oxidase From Hansenula Polymorpha, PDB code: 3loy was solved by V.J.Klema, B.J.Johnson, C.M.Wilmot, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	37.42 / 2.00
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	288.510, 91.065, 151.098, 90.00, 117.23, 90.00
R / Rfree (%)	14.5 / 19.1

The binding sites of Copper atom in the Crystal Structure of A Copper-Containing Benzylamine Oxidase From Hansenula Polymorpha (pdb code 3loy). 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 A Copper-Containing Benzylamine Oxidase From Hansenula Polymorpha, PDB code: 3loy:
Jump to Copper binding site number: 1; 2; 3;

Copper binding site 1 out of 3 in the Crystal Structure of A Copper-Containing Benzylamine Oxidase From Hansenula Polymorpha


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 A Copper-Containing Benzylamine Oxidase From Hansenula Polymorpha within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu635 b:22.7 occ:1.00 ND1 A:HIS597 2.0 22.0 1.0 NE2 A:HIS436 2.0 22.5 1.0 NE2 A:HIS438 2.1 23.3 1.0 O A:HOH1582 2.6 36.5 1.0 O A:HOH772 2.6 23.8 1.0 CE1 A:HIS597 3.0 17.6 1.0 CG A:HIS597 3.0 22.1 1.0 CE1 A:HIS436 3.0 21.6 1.0 CD2 A:HIS436 3.0 17.8 1.0 CD2 A:HIS438 3.0 17.8 1.0 CE1 A:HIS438 3.1 17.0 1.0 CB A:HIS597 3.3 19.1 1.0 NE2 A:HIS597 4.1 21.2 1.0 ND1 A:HIS436 4.1 18.2 1.0 CD2 A:HIS597 4.1 20.4 1.0 CG A:HIS436 4.1 19.8 1.0 CG A:HIS438 4.2 20.2 1.0 ND1 A:HIS438 4.2 18.5 1.0 CE1 A:PHE595 4.3 28.9 1.0 O A:HOH695 4.4 18.6 1.0 O2 A:TPQ386 4.4 29.5 1.0 CZ A:PHE595 4.8 25.4 1.0 O A:HOH644 4.9 30.0 1.0 CA A:HIS597 4.9 19.4 1.0 O A:HOH1387 5.0 40.5 1.0

Copper binding site 2 out of 3 in the Crystal Structure of A Copper-Containing Benzylamine Oxidase From Hansenula Polymorpha


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 A Copper-Containing Benzylamine Oxidase From Hansenula Polymorpha within 5.0Å range: probe atom residue distance (Å) B Occ B:Cu635 b:24.9 occ:1.00 NE2 B:HIS436 1.9 18.3 1.0 ND1 B:HIS597 2.1 20.2 1.0 NE2 B:HIS438 2.1 20.9 1.0 O B:HOH831 2.3 26.1 1.0 O B:HOH1321 2.5 52.4 1.0 CE1 B:HIS436 2.8 20.5 1.0 CD2 B:HIS436 2.9 21.6 1.0 CD2 B:HIS438 3.0 18.1 1.0 CG B:HIS597 3.0 23.5 1.0 CE1 B:HIS597 3.2 18.9 1.0 CE1 B:HIS438 3.2 24.2 1.0 CB B:HIS597 3.3 19.1 1.0 ND1 B:HIS436 3.9 23.5 1.0 CG B:HIS436 4.0 21.5 1.0 CG B:HIS438 4.2 22.3 1.0 CD2 B:HIS597 4.2 19.6 1.0 NE2 B:HIS597 4.2 22.6 1.0 ND1 B:HIS438 4.3 24.3 1.0 O B:HOH718 4.3 18.1 1.0 CE1 B:PHE595 4.4 27.1 1.0 O2 B:TPQ386 4.7 25.6 1.0 O B:HOH1330 4.8 44.9 1.0 O B:HOH1546 4.8 34.1 1.0 CA B:HIS597 4.8 21.5 1.0 CZ B:PHE595 4.8 23.6 1.0

Copper binding site 3 out of 3 in the Crystal Structure of A Copper-Containing Benzylamine Oxidase From Hansenula Polymorpha


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 A Copper-Containing Benzylamine Oxidase From Hansenula Polymorpha within 5.0Å range: probe atom residue distance (Å) B Occ C:Cu635 b:21.2 occ:1.00 NE2 C:HIS438 2.0 19.9 1.0 NE2 C:HIS436 2.0 15.7 1.0 ND1 C:HIS597 2.0 17.9 1.0 O C:HOH884 2.4 39.9 1.0 O C:HOH653 2.5 22.0 1.0 CE1 C:HIS436 3.0 15.1 1.0 CE1 C:HIS438 3.0 21.9 1.0 CE1 C:HIS597 3.0 14.9 1.0 CD2 C:HIS438 3.0 18.2 1.0 CD2 C:HIS436 3.0 17.5 1.0 CG C:HIS597 3.0 20.2 1.0 CB C:HIS597 3.3 19.1 1.0 ND1 C:HIS436 4.1 15.6 1.0 ND1 C:HIS438 4.1 17.9 1.0 NE2 C:HIS597 4.1 16.7 1.0 CG C:HIS436 4.1 17.2 1.0 CG C:HIS438 4.1 19.8 1.0 CD2 C:HIS597 4.2 16.3 1.0 CE1 C:PHE595 4.3 23.6 1.0 O C:HOH861 4.4 19.3 1.0 O2 C:TPQ386 4.5 22.5 1.0 CZ C:PHE595 4.7 22.1 1.0 O C:HOH1687 4.8 46.0 1.0 CA C:HIS597 4.8 18.4 1.0 O C:HOH889 4.9 27.4 1.0 CD2 C:LEU410 4.9 15.0 1.0

C.M.Chang, V.J.Klema, B.J.Johnson, M.Mure, J.P.Klinman, C.M.Wilmot. Kinetic and Structural Analysis of Substrate Specificity in Two Copper Amine Oxidases From Hansenula Polymorpha. Biochemistry V. 49 2540 2010.
ISSN: ISSN 0006-2960
PubMed: 20155950
DOI: 10.1021/BI901933D