Cobalt in PDB 3oqe: Structure of Opda Mutant Y257F

All present enzymatic activity of Structure of Opda Mutant Y257F:
3.1.8.1;

The structure of Structure of Opda Mutant Y257F, PDB code: 3oqe was solved by F.Ely, L.W.Guddat, D.L.Ollis, G.Schenk, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	21.67 / 1.90
Space group	P 31 2 1
Cell size a, b, c (Å), α, β, γ (°)	109.048, 109.048, 62.231, 90.00, 90.00, 120.00
R / Rfree (%)	17.6 / 22.8

The binding sites of Cobalt atom in the Structure of Opda Mutant Y257F (pdb code 3oqe). This binding sites where shown within 5.0 Angstroms radius around Cobalt atom.
In total 2 binding sites of Cobalt where determined in the Structure of Opda Mutant Y257F, PDB code: 3oqe:
Jump to Cobalt binding site number: 1; 2;

Cobalt binding site 1 out of 2 in the Structure of Opda Mutant Y257F


Mono view


Stereo pair view

A full contact list of Cobalt with other atoms in the Co binding site number 1 of Structure of Opda Mutant Y257F within 5.0Å range: probe atom residue distance (Å) B Occ A:Co800 b:18.0 occ:1.00 O A:HOH401 2.0 19.9 1.0 NE2 A:HIS57 2.1 14.7 1.0 OQ1 A:KCX169 2.1 9.2 0.8 NE2 A:HIS55 2.2 15.9 1.0 OD1 A:ASP301 2.2 14.1 1.0 C1 A:EDO702 2.9 23.9 1.0 CE1 A:HIS57 3.0 16.2 1.0 CX A:KCX169 3.0 11.6 0.8 CD2 A:HIS55 3.0 16.8 1.0 CG A:ASP301 3.1 14.2 1.0 CD2 A:HIS57 3.1 15.0 1.0 O1 A:EDO702 3.2 8.4 1.0 CE1 A:HIS55 3.2 13.4 1.0 OD2 A:ASP301 3.4 15.8 1.0 OQ2 A:KCX169 3.5 10.6 0.8 CO A:CO801 3.8 19.2 1.0 NZ A:KCX169 4.1 15.2 1.0 CG2 A:VAL101 4.1 13.0 1.0 O2 A:EDO702 4.1 35.0 1.0 ND1 A:HIS57 4.1 15.8 1.0 C2 A:EDO702 4.2 29.6 1.0 CG A:HIS57 4.2 14.8 1.0 CE1 A:HIS230 4.2 13.5 1.0 CG A:HIS55 4.2 14.4 1.0 ND1 A:HIS55 4.3 15.9 1.0 O A:HOH402 4.3 17.8 1.0 CB A:ASP301 4.4 12.7 1.0 NE2 A:HIS230 4.5 14.9 1.0 O A:HOH1 4.6 26.2 1.0 CA A:ASP301 4.8 13.0 1.0

Cobalt binding site 2 out of 2 in the Structure of Opda Mutant Y257F


Mono view


Stereo pair view

A full contact list of Cobalt with other atoms in the Co binding site number 2 of Structure of Opda Mutant Y257F within 5.0Å range: probe atom residue distance (Å) B Occ A:Co801 b:19.2 occ:1.00 OQ2 A:KCX169 2.0 10.6 0.8 NE2 A:HIS230 2.1 14.9 1.0 ND1 A:HIS201 2.1 14.8 1.0 O A:HOH402 2.2 17.8 1.0 O A:HOH401 2.4 19.9 1.0 O1 A:EDO702 3.0 8.4 1.0 CD2 A:HIS230 3.0 13.3 1.0 CE1 A:HIS201 3.0 16.2 1.0 CX A:KCX169 3.0 11.6 0.8 CE1 A:HIS230 3.1 13.5 1.0 CG A:HIS201 3.2 15.8 1.0 OQ1 A:KCX169 3.4 9.2 0.8 CB A:HIS201 3.6 15.9 1.0 NH2 A:ARG254 3.6 12.9 0.5 CO A:CO800 3.8 18.0 1.0 NE1 A:TRP131 3.9 16.8 1.0 ND1 A:HIS230 4.2 11.9 1.0 CG A:HIS230 4.2 16.0 1.0 NE2 A:HIS201 4.2 16.1 1.0 NZ A:KCX169 4.2 15.2 1.0 CE1 A:HIS55 4.2 13.4 1.0 C1 A:EDO702 4.2 23.9 1.0 NE2 A:HIS55 4.2 15.9 1.0 CD2 A:HIS201 4.3 15.3 1.0 CA A:HIS201 4.3 15.6 1.0 OD2 A:ASP301 4.4 15.8 1.0 CZ A:ARG254 4.5 14.3 0.5 CD1 A:TRP131 4.5 16.5 1.0 CE A:KCX169 4.7 13.9 1.0 O A:HOH403 4.7 33.4 1.0 NE A:ARG254 5.0 14.7 0.5 O2 A:EDO702 5.0 35.0 1.0

F.Ely, K.S.Hadler, L.R.Gahan, L.W.Guddat, D.L.Ollis, G.Schenk. The Organophosphate-Degrading Enzyme From Agrobacterium Radiobacter Displays Mechanistic Flexibility For Catalysis. Biochem.J. V. 432 565 2010.
ISSN: ISSN 0264-6021
PubMed: 20868365
DOI: 10.1042/BJ20101054