Cobalt in PDB 3gu2: Y97L/G100-/E101- Mutant in Organophosphorus Hydrolase

The structure of Y97L/G100-/E101- Mutant in Organophosphorus Hydrolase, PDB code: 3gu2 was solved by R.Hawwa, S.Larsen, K.Ratia, A.Mesecar, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	20.00 / 2.00
Space group	P 31 2 1
Cell size a, b, c (Å), α, β, γ (°)	61.072, 61.072, 204.578, 90.00, 90.00, 120.00
R / Rfree (%)	22.1 / 28.4

The binding sites of Cobalt atom in the Y97L/G100-/E101- Mutant in Organophosphorus Hydrolase (pdb code 3gu2). This binding sites where shown within 5.0 Angstroms radius around Cobalt atom.
In total 2 binding sites of Cobalt where determined in the Y97L/G100-/E101- Mutant in Organophosphorus Hydrolase, PDB code: 3gu2:
Jump to Cobalt binding site number: 1; 2;

Cobalt binding site 1 out of 2 in the Y97L/G100-/E101- Mutant in Organophosphorus Hydrolase


Mono view


Stereo pair view

A full contact list of Cobalt with other atoms in the Co binding site number 1 of Y97L/G100-/E101- Mutant in Organophosphorus Hydrolase within 5.0Å range: probe atom residue distance (Å) B Occ A:Co1 b:27.0 occ:1.00 NE2 A:HIS123 2.1 21.0 1.0 NE2 A:HIS121 2.2 21.4 1.0 OD1 A:ASP364 2.3 17.7 1.0 OQ2 A:KCX243 2.5 31.3 1.0 CE1 A:HIS123 2.9 22.6 1.0 O A:HOH9 3.0 22.3 1.0 CX A:KCX243 3.1 30.8 1.0 CG A:ASP364 3.1 17.7 1.0 OQ1 A:KCX243 3.1 28.1 1.0 CD2 A:HIS123 3.2 22.9 1.0 CE1 A:HIS121 3.2 20.7 1.0 CD2 A:HIS121 3.2 21.9 1.0 OD2 A:ASP364 3.4 22.2 1.0 CO A:CO2 3.4 32.4 1.0 O A:HOH46 4.1 29.5 1.0 ND1 A:HIS123 4.1 22.6 1.0 CG A:HIS123 4.2 23.2 1.0 CE1 A:HIS304 4.3 26.0 1.0 NZ A:KCX243 4.3 33.6 1.0 ND1 A:HIS121 4.3 21.3 1.0 NE2 A:HIS304 4.3 26.2 1.0 CG A:HIS121 4.4 23.0 1.0 CB A:ASP364 4.4 18.3 1.0 CB A:ALA167 4.8 19.9 1.0 CA A:ASP364 4.9 20.8 1.0 CE A:KCX243 4.9 32.7 1.0 O A:HOH671 5.0 50.8 1.0

Cobalt binding site 2 out of 2 in the Y97L/G100-/E101- Mutant in Organophosphorus Hydrolase


Mono view


Stereo pair view

A full contact list of Cobalt with other atoms in the Co binding site number 2 of Y97L/G100-/E101- Mutant in Organophosphorus Hydrolase within 5.0Å range: probe atom residue distance (Å) B Occ A:Co2 b:32.4 occ:1.00 OQ1 A:KCX243 1.8 28.1 1.0 NE2 A:HIS304 2.3 26.2 1.0 O A:HOH46 2.3 29.5 1.0 ND1 A:HIS276 2.3 28.6 1.0 O A:HOH671 2.5 50.8 1.0 CX A:KCX243 3.0 30.8 1.0 CD2 A:HIS304 3.2 26.1 1.0 CE1 A:HIS276 3.2 27.2 1.0 CE1 A:HIS304 3.3 26.0 1.0 CG A:HIS276 3.4 26.9 1.0 O A:HOH9 3.4 22.3 1.0 CO A:CO1 3.4 27.0 1.0 OQ2 A:KCX243 3.6 31.3 1.0 CB A:HIS276 3.7 25.8 1.0 NZ A:KCX243 4.0 33.6 1.0 OD2 A:ASP364 4.3 22.2 1.0 CG A:HIS304 4.3 24.3 1.0 ND1 A:HIS304 4.4 26.6 1.0 O A:HOH632 4.4 49.2 1.0 NE2 A:HIS276 4.4 28.1 1.0 NE2 A:HIS121 4.5 21.4 1.0 CD2 A:HIS276 4.5 28.3 1.0 CE1 A:HIS121 4.5 20.7 1.0 CA A:HIS276 4.6 24.3 1.0 NH1 A:ARG328 4.9 44.3 1.0 CG A:ASP364 4.9 17.7 1.0 OD1 A:ASP364 4.9 17.7 1.0

R.Hawwa, S.D.Larsen, K.Ratia, A.D.Mesecar. Structure-Based and Random Mutagenesis Approaches Increase the Organophosphate-Degrading Activity of A Phosphotriesterase Homologue From Deinococcus Radiodurans. J.Mol.Biol. V. 393 36 2009.
ISSN: ISSN 0022-2836
PubMed: 19631223
DOI: 10.1016/J.JMB.2009.06.083