Copper in PDB 2y74: The Crystal Structure of Human Soluble Primary Amine Oxidase AOC3 in the Off-Copper Conformation

All present enzymatic activity of The Crystal Structure of Human Soluble Primary Amine Oxidase AOC3 in the Off-Copper Conformation:
1.4.3.6;

The structure of The Crystal Structure of Human Soluble Primary Amine Oxidase AOC3 in the Off-Copper Conformation, PDB code: 2y74 was solved by H.Elovaara, H.Kidron, V.Parkash, Y.Nymalm, E.Bligt, P.Ollikka, D.J.Smith, M.Pihlavisto, M.Salmi, S.Jalkanen, T.A.Salminen, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	38.21 / 2.95
Space group	P 65 2 2
Cell size a, b, c (Å), α, β, γ (°)	225.800, 225.800, 218.700, 90.00, 90.00, 120.00
R / Rfree (%)	17.9 / 21.4

The structure of The Crystal Structure of Human Soluble Primary Amine Oxidase AOC3 in the Off-Copper Conformation also contains other interesting chemical elements:

Calcium

(Ca)

4 atoms

The binding sites of Copper atom in the The Crystal Structure of Human Soluble Primary Amine Oxidase AOC3 in the Off-Copper Conformation (pdb code 2y74). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total 2 binding sites of Copper where determined in the The Crystal Structure of Human Soluble Primary Amine Oxidase AOC3 in the Off-Copper Conformation, PDB code: 2y74:
Jump to Copper binding site number: 1; 2;

Copper binding site 1 out of 2 in the The Crystal Structure of Human Soluble Primary Amine Oxidase AOC3 in the Off-Copper Conformation


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of The Crystal Structure of Human Soluble Primary Amine Oxidase AOC3 in the Off-Copper Conformation within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu801 b:22.7 occ:1.00 ND1 A:HIS684 1.8 26.7 1.0 NE2 A:HIS522 1.8 25.1 1.0 NE2 A:HIS520 1.9 25.7 1.0 O A:HOH908 2.2 29.0 1.0 CE1 A:HIS684 2.7 24.8 1.0 CE1 A:HIS520 2.7 22.3 1.0 CD2 A:HIS522 2.8 20.8 1.0 CE1 A:HIS522 2.9 30.4 1.0 O A:HOH955 2.9 12.9 1.0 CD2 A:HIS520 3.0 22.1 1.0 CG A:HIS684 3.0 23.9 1.0 CB A:HIS684 3.5 22.3 1.0 NE2 A:HIS684 3.9 20.4 1.0 ND1 A:HIS520 3.9 23.4 1.0 CG A:HIS522 4.0 25.8 1.0 ND1 A:HIS522 4.0 33.0 1.0 CD2 A:HIS684 4.0 20.0 1.0 CG A:HIS520 4.0 16.6 1.0 O A:HOH939 4.0 26.3 1.0 O2 A:T0I471 4.3 46.3 1.0 CE2 A:PHE682 4.8 28.1 1.0 CA A:HIS684 4.9 18.5 1.0

Copper binding site 2 out of 2 in the The Crystal Structure of Human Soluble Primary Amine Oxidase AOC3 in the Off-Copper Conformation


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 2 of The Crystal Structure of Human Soluble Primary Amine Oxidase AOC3 in the Off-Copper Conformation within 5.0Å range: probe atom residue distance (Å) B Occ B:Cu801 b:31.0 occ:1.00 O B:HOH905 2.2 29.0 1.0 NE2 B:HIS520 2.2 24.9 1.0 ND1 B:HIS684 2.2 32.7 1.0 NE2 B:HIS522 2.4 31.9 1.0 CE1 B:HIS520 3.0 29.1 1.0 CE1 B:HIS684 3.1 34.4 1.0 CD2 B:HIS522 3.1 28.5 1.0 CG B:HIS684 3.2 33.9 1.0 O B:HOH968 3.2 17.0 1.0 CD2 B:HIS520 3.3 33.5 1.0 CE1 B:HIS522 3.6 32.8 1.0 CB B:HIS684 3.6 32.4 1.0 O2 B:T0I471 3.9 39.4 1.0 NE2 B:HIS684 4.2 33.9 1.0 ND1 B:HIS520 4.2 28.7 1.0 O B:HOH955 4.3 31.9 1.0 CD2 B:HIS684 4.3 28.5 1.0 CG B:HIS522 4.4 34.0 1.0 CG B:HIS520 4.4 24.0 1.0 ND1 B:HIS522 4.5 42.8 1.0 C2 B:T0I471 4.9 47.5 1.0 C3 B:T0I471 5.0 52.5 1.0 CE1 B:PHE682 5.0 28.2 1.0

H.Elovaara, H.Kidron, V.Parkash, Y.Nymalm, E.Bligt, P.Ollikka, D.J.Smith, M.Pihlavisto, M.Salmi, S.Jalkanen, T.A.Salminen. Identification of Two Imidazole Binding Sites and Key Residues For Substrate Specificity in Human Primary Amine Oxidase AOC3. Biochemistry V. 50 5507 2011.
ISSN: ISSN 0006-2960
PubMed: 21585208
DOI: 10.1021/BI200117Z