Cobalt in PDB 3ood: Structure of Opda Y257F Mutant Soaked with Diethyl 4-Methoxyphenyl Phosphate For 20 Hours.

All present enzymatic activity of Structure of Opda Y257F Mutant Soaked with Diethyl 4-Methoxyphenyl Phosphate For 20 Hours.:
3.1.8.1;

The structure of Structure of Opda Y257F Mutant Soaked with Diethyl 4-Methoxyphenyl Phosphate For 20 Hours., PDB code: 3ood 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)	17.27 / 1.89
Space group	P 31 2 1
Cell size a, b, c (Å), α, β, γ (°)	109.000, 109.000, 62.000, 90.00, 90.00, 120.00
R / Rfree (%)	15.5 / 19.5

The binding sites of Cobalt atom in the Structure of Opda Y257F Mutant Soaked with Diethyl 4-Methoxyphenyl Phosphate For 20 Hours. (pdb code 3ood). 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 Y257F Mutant Soaked with Diethyl 4-Methoxyphenyl Phosphate For 20 Hours., PDB code: 3ood:
Jump to Cobalt binding site number: 1; 2;

Cobalt binding site 1 out of 2 in the Structure of Opda Y257F Mutant Soaked with Diethyl 4-Methoxyphenyl Phosphate For 20 Hours.


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 Y257F Mutant Soaked with Diethyl 4-Methoxyphenyl Phosphate For 20 Hours. within 5.0Å range: probe atom residue distance (Å) B Occ A:Co800 b:12.3 occ:1.00 O1 A:EPL702 1.8 17.3 0.6 NE2 A:HIS57 2.1 9.0 1.0 NE2 A:HIS55 2.1 10.3 1.0 OQ1 A:KCX169 2.1 4.5 0.8 O A:HOH500 2.2 4.1 0.4 OD1 A:ASP301 2.2 9.8 1.0 O A:HOH434 2.8 7.4 0.4 CD2 A:HIS55 3.0 10.1 1.0 CE1 A:HIS57 3.0 10.2 1.0 CX A:KCX169 3.0 7.5 0.8 CG A:ASP301 3.1 8.9 1.0 CD2 A:HIS57 3.1 8.6 1.0 CE1 A:HIS55 3.2 8.9 1.0 P A:EPL702 3.2 11.6 0.6 OD2 A:ASP301 3.4 10.5 1.0 OQ2 A:KCX169 3.4 7.6 0.8 C10 A:EPL702 3.7 19.8 0.6 CO A:CO801 3.7 14.2 1.0 O4 A:EPL702 3.9 18.6 0.6 O A:HOH602 4.0 14.2 0.5 NZ A:KCX169 4.1 9.3 1.0 CG2 A:VAL101 4.1 7.5 1.0 ND1 A:HIS57 4.2 9.2 1.0 CE1 A:HIS230 4.2 9.2 1.0 O3 A:EPL702 4.2 9.9 0.3 O2 A:EPL702 4.2 26.6 0.4 CG A:HIS55 4.2 8.7 1.0 C11 A:EPL702 4.2 22.0 0.6 CG A:HIS57 4.2 9.7 1.0 ND1 A:HIS55 4.3 9.7 1.0 C11 A:EPL702 4.3 25.7 0.4 O2 A:EPL702 4.3 18.4 0.6 NE2 A:HIS230 4.4 9.9 1.0 CB A:ASP301 4.4 8.8 1.0 C8 A:EPL702 4.5 18.4 0.6 CA A:ASP301 4.8 8.6 1.0 O1 A:EPL702 4.9 26.1 0.4 C10 A:EPL702 4.9 25.2 0.4 O A:HOH435 4.9 16.3 0.5

Cobalt binding site 2 out of 2 in the Structure of Opda Y257F Mutant Soaked with Diethyl 4-Methoxyphenyl Phosphate For 20 Hours.


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 Y257F Mutant Soaked with Diethyl 4-Methoxyphenyl Phosphate For 20 Hours. within 5.0Å range: probe atom residue distance (Å) B Occ A:Co801 b:14.2 occ:1.00 OQ2 A:KCX169 1.9 7.6 0.8 NE2 A:HIS230 2.0 9.9 1.0 ND1 A:HIS201 2.1 8.6 1.0 O A:HOH500 2.1 4.1 0.4 O3 A:EPL702 2.3 9.9 0.3 O1 A:EPL702 2.9 17.3 0.6 P A:EPL702 3.0 11.6 0.6 CD2 A:HIS230 3.0 8.2 1.0 CX A:KCX169 3.0 7.5 0.8 CE1 A:HIS201 3.0 9.3 1.0 CE1 A:HIS230 3.0 9.2 1.0 CG A:HIS201 3.1 10.4 1.0 OQ1 A:KCX169 3.4 4.5 0.8 O1 A:EPL702 3.5 26.1 0.4 CB A:HIS201 3.5 10.2 1.0 NH2 A:ARG254 3.7 5.8 0.5 CO A:CO800 3.7 12.3 1.0 NE1 A:TRP131 3.9 11.1 1.0 O2 A:EPL702 4.0 18.4 0.6 ND1 A:HIS230 4.1 8.2 1.0 CE1 A:HIS55 4.1 8.9 1.0 NE2 A:HIS201 4.1 9.9 1.0 CG A:HIS230 4.1 10.0 1.0 NZ A:KCX169 4.1 9.3 1.0 NE2 A:HIS55 4.2 10.3 1.0 CD2 A:HIS201 4.2 9.0 1.0 CA A:HIS201 4.3 9.7 1.0 OD2 A:ASP301 4.3 10.5 1.0 O4 A:EPL702 4.4 18.6 0.6 CD1 A:TRP131 4.5 11.3 1.0 CZ A:ARG254 4.5 8.0 0.5 C8 A:EPL702 4.5 18.4 0.6 O A:HOH434 4.6 7.4 0.4 O A:HOH515 4.6 37.4 1.0 CE A:KCX169 4.6 10.3 1.0 O2 A:EPL702 4.7 26.6 0.4 P A:EPL702 4.7 25.1 0.4 NE A:ARG254 5.0 7.8 0.5

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