Nickel in PDB 1wmo: Crystal Structure of Topaquinone-Containing Amine Oxidase Activated By Nickel Ion

All present enzymatic activity of Crystal Structure of Topaquinone-Containing Amine Oxidase Activated By Nickel Ion:
1.4.3.6;

The structure of Crystal Structure of Topaquinone-Containing Amine Oxidase Activated By Nickel Ion, PDB code: 1wmo was solved by T.Okajima, S.Kishishita, Y.C.Chiu, T.Murakawa, M.Kim, H.Yamaguchi, S.Hirota, S.Kuroda, K.Tanizawa, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	10.00 / 1.80
Space group	I 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	157.679, 62.993, 183.670, 90.00, 111.83, 90.00
R / Rfree (%)	22.3 / 26.6

The binding sites of Nickel atom in the Crystal Structure of Topaquinone-Containing Amine Oxidase Activated By Nickel Ion (pdb code 1wmo). This binding sites where shown within 5.0 Angstroms radius around Nickel atom.
In total 2 binding sites of Nickel where determined in the Crystal Structure of Topaquinone-Containing Amine Oxidase Activated By Nickel Ion, PDB code: 1wmo:
Jump to Nickel binding site number: 1; 2;

Nickel binding site 1 out of 2 in the Crystal Structure of Topaquinone-Containing Amine Oxidase Activated By Nickel Ion


Mono view


Stereo pair view

A full contact list of Nickel with other atoms in the Ni binding site number 1 of Crystal Structure of Topaquinone-Containing Amine Oxidase Activated By Nickel Ion within 5.0Å range: probe atom residue distance (Å) B Occ A:Ni1001 b:13.2 occ:1.00 O A:HOH1418 1.8 6.0 1.0 NE2 A:HIS431 2.1 9.9 1.0 O A:HOH1276 2.1 11.7 1.0 O A:HOH1269 2.2 9.0 1.0 NE2 A:HIS433 2.3 16.6 1.0 ND1 A:HIS592 2.3 8.3 1.0 CE1 A:HIS431 3.0 8.9 1.0 CD2 A:HIS431 3.1 5.8 1.0 CD2 A:HIS433 3.1 14.6 1.0 CE1 A:HIS592 3.1 12.7 1.0 CE1 A:HIS433 3.3 15.8 1.0 CG A:HIS592 3.3 9.4 1.0 CB A:HIS592 3.7 8.4 1.0 ND1 A:HIS431 4.1 9.8 1.0 O A:HOH1273 4.2 19.3 1.0 CG A:HIS431 4.2 8.3 1.0 O A:HOH1302 4.2 12.9 1.0 NE2 A:HIS592 4.3 6.0 1.0 O A:HOH1182 4.3 10.4 1.0 CG A:HIS433 4.3 14.7 1.0 ND1 A:HIS433 4.4 12.1 1.0 CD2 A:HIS592 4.4 6.7 1.0 O2 A:TPQ382 4.5 17.7 1.0 SD A:MET602 4.5 18.2 1.0 O A:HOH1272 4.6 15.0 1.0 CE A:MET602 4.6 18.0 1.0

Nickel binding site 2 out of 2 in the Crystal Structure of Topaquinone-Containing Amine Oxidase Activated By Nickel Ion


Mono view


Stereo pair view

A full contact list of Nickel with other atoms in the Ni binding site number 2 of Crystal Structure of Topaquinone-Containing Amine Oxidase Activated By Nickel Ion within 5.0Å range: probe atom residue distance (Å) B Occ B:Ni1002 b:10.6 occ:1.00 O B:HOH1526 1.7 5.0 1.0 NE2 B:HIS431 2.0 7.4 1.0 O B:HOH1320 2.2 11.9 1.0 NE2 B:HIS433 2.2 13.5 1.0 ND1 B:HIS592 2.2 6.5 1.0 O B:HOH1317 2.3 11.2 1.0 CE1 B:HIS431 3.0 6.8 1.0 CD2 B:HIS431 3.0 5.1 1.0 CD2 B:HIS433 3.1 11.8 1.0 CE1 B:HIS592 3.1 12.0 1.0 CE1 B:HIS433 3.3 13.3 1.0 CG B:HIS592 3.3 10.8 1.0 CB B:HIS592 3.7 8.2 1.0 ND1 B:HIS431 4.1 7.1 1.0 CG B:HIS431 4.2 6.1 1.0 O B:HOH1176 4.3 17.1 1.0 O B:HOH1331 4.3 9.3 1.0 NE2 B:HIS592 4.3 5.1 1.0 CG B:HIS433 4.3 11.7 1.0 O B:HOH1104 4.3 9.2 1.0 ND1 B:HIS433 4.3 12.8 1.0 SD B:MET602 4.4 17.5 1.0 O2 B:TPQ382 4.4 15.4 1.0 CD2 B:HIS592 4.4 4.9 1.0 O B:HOH1322 4.7 13.2 1.0 CE B:MET602 4.9 13.2 1.0

T.Okajima, S.Kishishita, Y.C.Chiu, T.Murakawa, M.Kim, H.Yamaguchi, S.Hirota, S.Kuroda, K.Tanizawa. Reinvestigation of Metal Ion Specificity For Quinone Cofactor Biogenesis in Bacterial Copper Amine Oxidase Biochemistry V. 44 12041 2005.
ISSN: ISSN 0006-2960
PubMed: 16142901
DOI: 10.1021/BI051070R