Calcium in PDB 1tu5: Crystal Structure of Bovine Plasma Copper-Containing Amine Oxidase

All present enzymatic activity of Crystal Structure of Bovine Plasma Copper-Containing Amine Oxidase:
1.4.3.6;

The structure of Crystal Structure of Bovine Plasma Copper-Containing Amine Oxidase, PDB code: 1tu5 was solved by M.Lunelli, M.L.Di Paolo, M.Biadene, V.Calderone, M.Scarpa, R.Battistutta, A.Rigo, G.Zanotti, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	25.00 / 2.37
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	77.680, 131.192, 134.001, 90.00, 90.00, 90.00
R / Rfree (%)	20.5 / 23.7

The structure of Crystal Structure of Bovine Plasma Copper-Containing Amine Oxidase also contains other interesting chemical elements:

Copper	(Cu)	2 atoms
Chlorine	(Cl)	3 atoms

The binding sites of Calcium atom in the Crystal Structure of Bovine Plasma Copper-Containing Amine Oxidase (pdb code 1tu5). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total 4 binding sites of Calcium where determined in the Crystal Structure of Bovine Plasma Copper-Containing Amine Oxidase, PDB code: 1tu5:
Jump to Calcium binding site number: 1; 2; 3; 4;

Calcium binding site 1 out of 4 in the Crystal Structure of Bovine Plasma Copper-Containing Amine Oxidase


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Crystal Structure of Bovine Plasma Copper-Containing Amine Oxidase within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca902 b:19.0 occ:1.00 OD1 A:ASP672 2.3 23.4 1.0 OD1 A:ASP528 2.4 19.3 1.0 O A:LEU529 2.4 22.6 1.0 O A:LEU673 2.4 22.9 1.0 O A:HOH931 2.5 13.2 1.0 OD1 A:ASP530 2.5 20.7 1.0 C A:LEU529 3.4 21.2 1.0 N A:LEU673 3.4 22.8 1.0 C A:LEU673 3.5 22.4 1.0 CG A:ASP528 3.6 20.3 1.0 CG A:ASP672 3.6 23.1 1.0 CG A:ASP530 3.7 19.2 1.0 NZ A:LYS105 4.0 18.7 1.0 CA A:LEU673 4.0 22.7 1.0 CA A:ASP530 4.1 20.4 1.0 C A:ASP528 4.1 21.4 1.0 C A:ASP672 4.1 22.1 1.0 N A:ASP530 4.1 21.0 1.0 N A:LEU529 4.1 21.4 1.0 OD2 A:ASP528 4.2 20.8 1.0 O A:ASP528 4.3 22.8 1.0 CA A:ASP672 4.3 22.1 1.0 OD2 A:ASP672 4.3 21.4 1.0 CA A:LEU529 4.4 21.4 1.0 CB A:ASP530 4.5 19.9 1.0 CA A:ASP528 4.5 21.7 1.0 OD2 A:ASP530 4.6 22.6 1.0 O A:LEU534 4.6 28.9 1.0 CB A:ASP672 4.6 21.4 1.0 N A:VAL674 4.6 21.2 1.0 CB A:ASP528 4.7 20.3 1.0 OD1 A:ASN536 4.7 18.0 1.0 CB A:LEU673 4.7 23.3 1.0 CG2 A:VAL674 4.9 24.0 1.0 CA A:VAL674 5.0 21.9 1.0 O A:ASP672 5.0 20.9 1.0

Calcium binding site 2 out of 4 in the Crystal Structure of Bovine Plasma Copper-Containing Amine Oxidase


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 2 of Crystal Structure of Bovine Plasma Copper-Containing Amine Oxidase within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca903 b:19.6 occ:1.00 OD1 A:ASN664 2.4 31.7 1.0 OE1 A:GLU666 2.4 31.3 1.0 OE1 A:GLU571 2.5 27.4 1.0 O A:PHE662 2.5 23.9 1.0 O A:HOH934 2.6 13.1 1.0 OE2 A:GLU571 2.6 22.9 1.0 O A:HOH976 2.6 16.4 1.0 CD A:GLU571 2.9 26.6 1.0 CD A:GLU666 3.4 33.2 1.0 CG A:ASN664 3.7 34.4 1.0 C A:PHE662 3.7 24.2 1.0 CG A:GLU666 3.9 30.1 1.0 NZ A:LYS637 4.1 22.1 1.0 N A:ASN664 4.1 30.0 1.0 CB A:GLU666 4.3 28.3 1.0 OE2 A:GLU666 4.3 34.2 1.0 CG A:GLU571 4.4 26.9 1.0 ND2 A:ASN664 4.4 35.6 1.0 OE2 A:GLU640 4.5 22.5 1.0 CA A:PHE662 4.5 22.7 1.0 CE A:LYS637 4.6 22.1 1.0 N A:GLN635 4.6 22.4 1.0 N A:ILE663 4.7 25.4 1.0 CB A:THR634 4.7 20.0 1.0 CB A:ASN664 4.7 33.2 1.0 CA A:ILE663 4.8 26.0 1.0 OE1 A:GLU640 4.8 23.1 1.0 CA A:ASN664 4.9 32.5 1.0 C A:ILE663 4.9 27.9 1.0 CB A:GLN635 5.0 23.9 1.0 CD A:LYS637 5.0 22.3 1.0

Calcium binding site 3 out of 4 in the Crystal Structure of Bovine Plasma Copper-Containing Amine Oxidase


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 3 of Crystal Structure of Bovine Plasma Copper-Containing Amine Oxidase within 5.0Å range: probe atom residue distance (Å) B Occ B:Ca1902 b:23.3 occ:1.00 OD1 B:ASP672 2.4 23.4 1.0 O B:LEU529 2.4 21.8 1.0 OD1 B:ASP528 2.4 19.9 1.0 OD1 B:ASP530 2.4 17.8 1.0 O B:HOH1995 2.4 17.5 1.0 O B:LEU673 2.5 24.6 1.0 C B:LEU529 3.4 21.8 1.0 N B:LEU673 3.4 24.0 1.0 C B:LEU673 3.5 22.2 1.0 CG B:ASP528 3.6 21.9 1.0 CG B:ASP672 3.6 23.6 1.0 CG B:ASP530 3.6 19.5 1.0 NZ B:LYS105 3.8 17.6 1.0 CA B:LEU673 4.0 23.1 1.0 CA B:ASP530 4.1 17.2 1.0 N B:ASP530 4.1 16.2 1.0 C B:ASP528 4.1 21.7 1.0 C B:ASP672 4.1 23.4 1.0 N B:LEU529 4.2 21.1 1.0 OD2 B:ASP528 4.3 19.7 1.0 O B:ASP528 4.3 20.9 1.0 CA B:ASP672 4.4 22.9 1.0 OD2 B:ASP672 4.4 25.6 1.0 CA B:LEU529 4.5 21.7 1.0 CB B:ASP530 4.5 16.6 1.0 OD2 B:ASP530 4.5 19.7 1.0 CA B:ASP528 4.6 21.1 1.0 O B:LEU534 4.6 26.9 1.0 CB B:ASP672 4.6 23.5 1.0 N B:VAL674 4.7 22.9 1.0 OD1 B:ASN536 4.7 16.7 1.0 CB B:ASP528 4.7 21.1 1.0 CB B:LEU673 4.8 22.1 1.0

Calcium binding site 4 out of 4 in the Crystal Structure of Bovine Plasma Copper-Containing Amine Oxidase


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 4 of Crystal Structure of Bovine Plasma Copper-Containing Amine Oxidase within 5.0Å range: probe atom residue distance (Å) B Occ B:Ca1903 b:23.5 occ:1.00 OD1 B:ASN664 2.4 30.9 1.0 OE1 B:GLU571 2.4 28.1 1.0 OE1 B:GLU666 2.4 34.6 1.0 O B:HOH2029 2.5 22.2 1.0 O B:PHE662 2.5 23.6 1.0 O B:HOH1952 2.5 7.5 1.0 OE2 B:GLU571 2.6 30.6 1.0 CD B:GLU571 2.8 29.4 1.0 CD B:GLU666 3.4 35.0 1.0 CG B:ASN664 3.6 31.4 1.0 C B:PHE662 3.6 24.2 1.0 CG B:GLU666 3.8 33.1 1.0 NZ B:LYS637 4.1 19.4 1.0 N B:ASN664 4.1 28.4 1.0 CB B:GLU666 4.2 29.6 1.0 CG B:GLU571 4.4 28.1 1.0 ND2 B:ASN664 4.4 31.8 1.0 OE2 B:GLU666 4.4 36.1 1.0 CA B:PHE662 4.5 22.4 1.0 CB B:THR634 4.6 20.9 1.0 N B:ILE663 4.6 24.9 1.0 O B:HOH1973 4.6 24.6 1.0 CE B:LYS637 4.6 20.2 1.0 CA B:ILE663 4.6 24.6 1.0 N B:GLN635 4.7 23.6 1.0 OE2 B:GLU640 4.7 21.9 1.0 CB B:ASN664 4.7 30.5 1.0 OE1 B:GLU640 4.8 23.4 1.0 CA B:ASN664 4.8 30.8 1.0 C B:ILE663 4.9 25.8 1.0 CG2 B:THR634 5.0 21.4 1.0

M.Lunelli, M.L.Di Paolo, M.Biadene, V.Calderone, R.Battistutta, M.Scarpa, A.Rigo, G.Zanotti. Crystal Structure of Amine Oxidase From Bovine Serum. J.Mol.Biol. V. 346 991 2005.
ISSN: ISSN 0022-2836
PubMed: 15701511
DOI: 10.1016/J.JMB.2004.12.038