Cobalt in PDB 1iqx: Crystal Structure of Cobalt-Substituted Amine Oxidase From Arthrobacter Globiformis

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

The structure of Crystal Structure of Cobalt-Substituted Amine Oxidase From Arthrobacter Globiformis, PDB code: 1iqx was solved by S.Kishishita, T.Okajima, M.Mure, M.Kim, H.Yamaguchi, S.Hirota, S.Suzuki, 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 / 2.00
Space group	I 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	157.990, 62.770, 184.190, 90.00, 111.85, 90.00
R / Rfree (%)	21.1 / 26

The binding sites of Cobalt atom in the Crystal Structure of Cobalt-Substituted Amine Oxidase From Arthrobacter Globiformis (pdb code 1iqx). This binding sites where shown within 5.0 Angstroms radius around Cobalt atom.
In total 2 binding sites of Cobalt where determined in the Crystal Structure of Cobalt-Substituted Amine Oxidase From Arthrobacter Globiformis, PDB code: 1iqx:
Jump to Cobalt binding site number: 1; 2;

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


Mono view


Stereo pair view

A full contact list of Cobalt with other atoms in the Co binding site number 1 of Crystal Structure of Cobalt-Substituted Amine Oxidase From Arthrobacter Globiformis within 5.0Å range: probe atom residue distance (Å) B Occ A:Co701 b:10.4 occ:1.00 O A:HOH957 2.0 8.2 1.0 NE2 A:HIS431 2.1 5.6 1.0 O A:HOH956 2.2 14.9 1.0 NE2 A:HIS433 2.3 12.7 1.0 ND1 A:HIS592 2.3 6.0 1.0 O A:HOH955 2.3 13.9 1.0 CE1 A:HIS431 3.1 6.4 1.0 CD2 A:HIS433 3.2 10.0 1.0 CD2 A:HIS431 3.2 4.7 1.0 CE1 A:HIS592 3.2 9.8 1.0 CE1 A:HIS433 3.3 13.2 1.0 CG A:HIS592 3.4 7.4 1.0 CB A:HIS592 3.8 5.4 1.0 O A:HOH958 4.2 11.2 1.0 ND1 A:HIS431 4.2 5.3 1.0 O A:HOH911 4.3 16.4 1.0 CG A:HIS431 4.3 4.7 1.0 SD A:MET602 4.3 22.6 1.0 CG A:HIS433 4.4 13.2 1.0 NE2 A:HIS592 4.4 7.5 1.0 ND1 A:HIS433 4.4 7.7 1.0 O A:HOH875 4.4 9.7 1.0 CD2 A:HIS592 4.5 7.4 1.0 O A:HOH878 4.6 14.6 1.0 O2 A:TPQ382 4.6 21.4 1.0 CE A:MET602 4.8 20.6 1.0

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


Mono view


Stereo pair view

A full contact list of Cobalt with other atoms in the Co binding site number 2 of Crystal Structure of Cobalt-Substituted Amine Oxidase From Arthrobacter Globiformis within 5.0Å range: probe atom residue distance (Å) B Occ B:Co701 b:9.6 occ:1.00 O B:HOH1012 2.0 8.5 1.0 NE2 B:HIS431 2.1 4.4 1.0 O B:HOH1015 2.2 13.6 1.0 ND1 B:HIS592 2.3 5.6 1.0 NE2 B:HIS433 2.3 12.0 1.0 O B:HOH1160 2.4 12.1 1.0 CD2 B:HIS431 3.1 2.8 1.0 CE1 B:HIS431 3.1 4.5 1.0 CE1 B:HIS592 3.1 10.4 1.0 CD2 B:HIS433 3.2 10.8 1.0 CE1 B:HIS433 3.4 15.0 1.0 CG B:HIS592 3.4 8.2 1.0 CB B:HIS592 3.8 7.6 1.0 ND1 B:HIS431 4.2 4.0 1.0 CG B:HIS431 4.2 2.1 1.0 O B:HOH874 4.2 22.2 1.0 NE2 B:HIS592 4.3 6.4 1.0 O B:HOH1013 4.3 9.4 1.0 O B:HOH802 4.4 8.4 1.0 CG B:HIS433 4.4 11.6 1.0 SD B:MET602 4.4 27.1 1.0 ND1 B:HIS433 4.4 9.2 1.0 CD2 B:HIS592 4.4 8.1 1.0 O2 B:TPQ382 4.6 23.5 1.0 O B:HOH1014 4.6 12.8 1.0 CE B:MET602 4.7 30.8 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