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

Enzymatic activity of 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;

Protein crystallography data

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

Other elements in 2y74:

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

Copper Binding Sites:

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 2y74

Go back to Copper Binding Sites List in 2y74
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 2y74

Go back to Copper Binding Sites List in 2y74
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

Reference:

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
Page generated: Sun Dec 13 11:07:55 2020

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