Cobalt in PDB 1wmp: Crystal Structure of Amine Oxidase Complexed with Cobalt Ion

All present enzymatic activity of Crystal Structure of Amine Oxidase Complexed with Cobalt Ion:
1.4.3.6;

The structure of Crystal Structure of Amine Oxidase Complexed with Cobalt Ion, PDB code: 1wmp 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 / 2.00
Space group	I 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	157.580, 63.376, 184.204, 90.00, 112.47, 90.00
R / Rfree (%)	18.8 / 22

The binding sites of Cobalt atom in the Crystal Structure of Amine Oxidase Complexed with Cobalt Ion (pdb code 1wmp). 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 Amine Oxidase Complexed with Cobalt Ion, PDB code: 1wmp:
Jump to Cobalt binding site number: 1; 2;

Cobalt binding site 1 out of 2 in the Crystal Structure of Amine Oxidase Complexed with Cobalt Ion


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 Amine Oxidase Complexed with Cobalt Ion within 5.0Å range: probe atom residue distance (Å) B Occ A:Co1001 b:45.8 occ:1.00 NE2 A:HIS431 2.1 19.3 1.0 NE2 A:HIS433 2.2 18.8 1.0 ND1 A:HIS592 2.3 22.9 1.0 OH A:TYR382 2.6 31.9 1.0 CD2 A:HIS433 3.0 16.9 1.0 CD2 A:HIS431 3.1 18.2 1.0 CE1 A:HIS431 3.1 19.5 1.0 CG A:HIS592 3.3 23.0 1.0 CE1 A:HIS433 3.3 17.5 1.0 CE1 A:HIS592 3.3 22.3 1.0 CZ A:TYR382 3.4 28.0 1.0 CB A:HIS592 3.5 20.4 1.0 CE2 A:TYR382 4.0 28.5 1.0 CE1 A:TYR382 4.1 29.0 1.0 ND1 A:HIS431 4.2 18.6 1.0 CG A:HIS431 4.2 19.8 1.0 CG A:HIS433 4.2 19.0 1.0 ND1 A:HIS433 4.3 16.5 1.0 O A:HOH1215 4.4 27.8 1.0 NE2 A:HIS592 4.4 21.7 1.0 CD2 A:HIS592 4.4 21.9 1.0 SD A:MET602 4.7 30.8 1.0 CE A:MET602 4.9 35.5 1.0

Cobalt binding site 2 out of 2 in the Crystal Structure of Amine Oxidase Complexed with Cobalt Ion


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 Amine Oxidase Complexed with Cobalt Ion within 5.0Å range: probe atom residue distance (Å) B Occ B:Co1002 b:49.4 occ:1.00 NE2 B:HIS431 2.2 17.9 1.0 NE2 B:HIS433 2.2 19.6 1.0 ND1 B:HIS592 2.3 21.4 1.0 OH B:TYR382 2.8 24.6 1.0 CD2 B:HIS433 2.9 17.4 1.0 CD2 B:HIS431 3.1 16.0 1.0 CE1 B:HIS431 3.1 17.3 1.0 CE1 B:HIS592 3.2 21.4 1.0 CG B:HIS592 3.3 19.9 1.0 CE1 B:HIS433 3.4 17.7 1.0 CZ B:TYR382 3.5 23.4 1.0 CB B:HIS592 3.6 17.1 1.0 CE2 B:TYR382 4.0 22.1 1.0 CE1 B:TYR382 4.2 23.0 1.0 CG B:HIS433 4.2 17.2 1.0 ND1 B:HIS431 4.2 16.9 1.0 CG B:HIS431 4.2 16.9 1.0 NE2 B:HIS592 4.3 22.1 1.0 CD2 B:HIS592 4.4 19.2 1.0 ND1 B:HIS433 4.4 16.3 1.0 SD B:MET602 4.5 25.7 1.0 O B:HOH1190 4.6 21.3 1.0 CE B:MET602 4.7 32.9 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