Nickel in PDB 1iqy: Crystal Structure of Nickel-Substituted Amine Oxidase From Arthrobacter Globiformis

All present enzymatic activity of Crystal Structure of Nickel-Substituted Amine Oxidase From Arthrobacter Globiformis:
1.4.3.6;

The structure of Crystal Structure of Nickel-Substituted Amine Oxidase From Arthrobacter Globiformis, PDB code: 1iqy was solved by S.Kishishita, T.Okajima, M.Mure, 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 (°)	157.800, 62.840, 184.070, 90.00, 111.80, 90.00
R / Rfree (%)	20.8 / 26

The binding sites of Nickel atom in the Crystal Structure of Nickel-Substituted Amine Oxidase From Arthrobacter Globiformis (pdb code 1iqy). 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 Nickel-Substituted Amine Oxidase From Arthrobacter Globiformis, PDB code: 1iqy:
Jump to Nickel binding site number: 1; 2;

Nickel binding site 1 out of 2 in the Crystal Structure of Nickel-Substituted Amine Oxidase From Arthrobacter Globiformis


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 Nickel-Substituted Amine Oxidase From Arthrobacter Globiformis within 5.0Å range: probe atom residue distance (Å) B Occ A:Ni701 b:14.2 occ:1.00 O A:HOH954 2.0 4.5 1.0 NE2 A:HIS431 2.0 3.0 1.0 O A:HOH953 2.1 23.6 1.0 NE2 A:HIS433 2.3 21.9 1.0 O A:HOH952 2.3 16.6 1.0 ND1 A:HIS592 2.4 10.3 1.0 CE1 A:HIS431 3.0 4.2 1.0 CD2 A:HIS431 3.0 6.3 1.0 CD2 A:HIS433 3.2 20.5 1.0 CE1 A:HIS433 3.2 23.7 1.0 CE1 A:HIS592 3.2 15.2 1.0 CG A:HIS592 3.4 12.4 1.0 CB A:HIS592 3.8 13.4 1.0 CE A:MET602 3.9 35.8 1.0 ND1 A:HIS431 4.1 4.6 1.0 CG A:HIS431 4.2 2.0 1.0 O A:HOH872 4.3 13.4 1.0 O A:HOH955 4.3 19.7 1.0 O A:HOH906 4.3 17.6 1.0 ND1 A:HIS433 4.3 19.1 1.0 CG A:HIS433 4.3 21.1 1.0 NE2 A:HIS592 4.4 10.1 1.0 O2 A:TPQ382 4.5 32.1 1.0 SD A:MET602 4.5 26.0 1.0 CD2 A:HIS592 4.5 13.2 1.0 O A:HOH876 4.7 18.2 1.0

Nickel binding site 2 out of 2 in the Crystal Structure of Nickel-Substituted Amine Oxidase From Arthrobacter Globiformis


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 Nickel-Substituted Amine Oxidase From Arthrobacter Globiformis within 5.0Å range: probe atom residue distance (Å) B Occ B:Ni701 b:12.5 occ:1.00 O B:HOH1014 2.0 5.5 1.0 NE2 B:HIS431 2.1 4.1 1.0 O B:HOH1017 2.2 19.1 1.0 NE2 B:HIS433 2.3 16.9 1.0 ND1 B:HIS592 2.3 8.0 1.0 O B:HOH1143 2.3 18.7 1.0 CD2 B:HIS431 3.0 8.8 1.0 CE1 B:HIS431 3.1 4.5 1.0 CD2 B:HIS433 3.1 15.5 1.0 CE1 B:HIS592 3.2 13.4 1.0 CG B:HIS592 3.3 12.1 1.0 CE1 B:HIS433 3.3 17.1 1.0 CB B:HIS592 3.7 11.4 1.0 ND1 B:HIS431 4.2 5.7 1.0 CG B:HIS431 4.2 4.2 1.0 O B:HOH880 4.2 24.5 1.0 O B:HOH805 4.2 10.3 1.0 CG B:HIS433 4.3 14.7 1.0 NE2 B:HIS592 4.3 8.8 1.0 ND1 B:HIS433 4.4 15.4 1.0 O B:HOH1015 4.4 14.5 1.0 SD B:MET602 4.4 30.7 1.0 CD2 B:HIS592 4.4 11.2 1.0 O2 B:TPQ382 4.5 29.1 1.0 O B:HOH1016 4.5 19.7 1.0 CE B:MET602 5.0 27.8 1.0

S.Kishishita, T.Okajima, M.Kim, H.Yamaguchi, S.Hirota, S.Suzuki, S.Kuroda, K.Tanizawa, M.Mure. Role of Copper Ion in Bacterial Copper Amine Oxidase: Spectroscopic and Crystallographic Studies of Metal-Substituted Enzymes J.Am.Chem.Soc. V. 125 1041 2003.
ISSN: ISSN 0002-7863
PubMed: 12537504
DOI: 10.1021/JA017899K