Cobalt in PDB 4wgx: Crystal Structure of Molinate Hydrolase

The structure of Crystal Structure of Molinate Hydrolase, PDB code: 4wgx was solved by E.Sugrue, P.D.Carr, N.J.Fraser, D.H.Hopkins, C.J.Jackson, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	41.62 / 2.29
Space group	I 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	126.429, 226.317, 265.382, 90.00, 90.00, 90.00
R / Rfree (%)	17.6 / 20.3

The binding sites of Cobalt atom in the Crystal Structure of Molinate Hydrolase (pdb code 4wgx). This binding sites where shown within 5.0 Angstroms radius around Cobalt atom.
In total 5 binding sites of Cobalt where determined in the Crystal Structure of Molinate Hydrolase, PDB code: 4wgx:
Jump to Cobalt binding site number: 1; 2; 3; 4; 5;

Cobalt binding site 1 out of 5 in the Crystal Structure of Molinate Hydrolase


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 Molinate Hydrolase within 5.0Å range: probe atom residue distance (Å) B Occ A:Co503 b:65.9 occ:1.00 O A:HOH831 1.9 68.9 1.0 O A:HOH823 2.1 46.7 1.0 NE2 A:HIS360 2.3 48.5 1.0 O A:HOH824 2.5 54.4 1.0 O A:HOH826 2.5 63.5 1.0 O A:HOH825 3.0 55.6 1.0 CD2 A:HIS360 3.1 35.4 1.0 HD2 A:HIS360 3.1 42.5 1.0 CE1 A:HIS360 3.4 42.5 1.0 HE1 A:HIS360 3.6 51.0 1.0 HG3 A:GLU361 3.8 43.1 1.0 OE2 A:GLU361 3.9 41.0 1.0 O A:HOH732 4.2 41.5 1.0 CG A:HIS360 4.3 33.3 1.0 ND1 A:HIS360 4.4 41.4 1.0 O A:HOH836 4.4 68.5 1.0 O A:HOH755 4.5 61.7 1.0 CG A:GLU361 4.5 35.9 1.0 CD A:GLU361 4.7 38.7 1.0 HG2 A:GLU361 4.7 43.1 1.0

Cobalt binding site 2 out of 5 in the Crystal Structure of Molinate Hydrolase


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 Molinate Hydrolase within 5.0Å range: probe atom residue distance (Å) B Occ A:Co504 b:0.5 occ:1.00 O A:HOH830 2.0 88.2 1.0 HE2 A:HIS45 2.0 0.2 1.0 O A:HOH829 2.3 92.1 1.0 O A:HOH827 2.3 98.9 1.0 HE1 A:HIS45 2.5 0.3 1.0 NE2 A:HIS45 2.6 1.0 1.0 O A:HOH828 2.8 91.8 1.0 CE1 A:HIS45 2.8 0.2 1.0 OE2 A:GLU43 3.0 0.3 1.0 CD2 A:HIS45 3.9 0.7 1.0 CD A:GLU43 3.9 0.7 1.0 ND1 A:HIS45 4.1 0.7 1.0 OE1 A:GLU43 4.3 0.1 1.0 HD2 A:HIS45 4.4 0.5 1.0 CG A:HIS45 4.6 0.2 1.0 HG2 A:GLU43 5.0 0.7 1.0

Cobalt binding site 3 out of 5 in the Crystal Structure of Molinate Hydrolase


Mono view


Stereo pair view

A full contact list of Cobalt with other atoms in the Co binding site number 3 of Crystal Structure of Molinate Hydrolase within 5.0Å range: probe atom residue distance (Å) B Occ B:Co502 b:72.9 occ:1.00 O B:HOH763 2.1 65.0 1.0 O B:HOH810 2.1 63.3 1.0 O B:HOH811 2.2 56.8 1.0 NE2 B:HIS360 2.3 48.4 1.0 O B:HOH809 2.4 61.4 1.0 O B:HOH808 2.6 58.5 1.0 CD2 B:HIS360 3.1 40.0 1.0 HD2 B:HIS360 3.2 48.0 1.0 CE1 B:HIS360 3.3 49.6 1.0 O B:HOH819 3.5 66.8 1.0 HE1 B:HIS360 3.6 59.6 1.0 HG3 B:GLU361 3.7 45.6 1.0 OE2 B:GLU361 3.8 50.8 1.0 O B:HOH800 4.3 39.1 1.0 CG B:HIS360 4.3 41.0 1.0 ND1 B:HIS360 4.4 43.6 1.0 CG B:GLU361 4.4 38.0 1.0 CD B:GLU361 4.6 39.9 1.0 O B:HOH725 4.6 64.1 1.0 HG2 B:GLU361 4.6 45.6 1.0

Cobalt binding site 4 out of 5 in the Crystal Structure of Molinate Hydrolase


Mono view


Stereo pair view

A full contact list of Cobalt with other atoms in the Co binding site number 4 of Crystal Structure of Molinate Hydrolase within 5.0Å range: probe atom residue distance (Å) B Occ C:Co502 b:66.5 occ:1.00 NE2 C:HIS360 2.2 51.0 1.0 O C:HOH731 2.4 58.7 1.0 O C:HOH737 2.4 58.4 1.0 O C:HOH738 2.4 61.3 1.0 O C:HOH681 2.5 54.3 1.0 O C:HOH753 2.6 63.3 1.0 O C:HOH741 2.6 49.9 1.0 CD2 C:HIS360 3.0 38.2 1.0 HD2 C:HIS360 3.0 45.9 1.0 CE1 C:HIS360 3.4 59.5 1.0 HE1 C:HIS360 3.7 71.4 1.0 HG3 C:GLU361 3.8 48.4 1.0 OE2 C:GLU361 4.0 47.1 1.0 O C:HOH745 4.2 53.6 1.0 O C:HOH747 4.2 65.5 1.0 CG C:HIS360 4.2 38.8 1.0 ND1 C:HIS360 4.4 48.8 1.0 HG2 C:GLU361 4.4 48.4 1.0 CG C:GLU361 4.5 40.3 1.0 CD C:GLU361 4.7 41.5 1.0

Cobalt binding site 5 out of 5 in the Crystal Structure of Molinate Hydrolase


Mono view


Stereo pair view

A full contact list of Cobalt with other atoms in the Co binding site number 5 of Crystal Structure of Molinate Hydrolase within 5.0Å range: probe atom residue distance (Å) B Occ D:Co502 b:84.2 occ:1.00 HE1 D:HIS360 1.6 86.0 1.0 O D:HOH703 1.9 74.8 1.0 O D:HOH702 2.1 80.1 1.0 O D:HOH700 2.4 64.9 1.0 O D:HOH698 2.4 61.3 1.0 O D:HOH701 2.4 73.0 1.0 CE1 D:HIS360 2.5 71.6 1.0 ND1 D:HIS360 3.2 61.2 1.0 NE2 D:HIS360 3.6 72.7 1.0 HG3 D:GLU361 3.8 82.5 1.0 HE2 D:HIS360 3.8 87.2 1.0 O D:HOH713 3.9 74.3 1.0 OE2 D:GLU361 4.1 67.3 1.0 CG D:HIS360 4.4 66.2 1.0 CD2 D:HIS360 4.6 53.8 1.0 CG D:GLU361 4.7 68.8 1.0 CD D:GLU361 4.8 65.5 1.0 HH21 D:ARG431 4.9 79.3 1.0 HG2 D:GLU361 5.0 82.5 1.0

E.Sugrue, N.J.Fraser, D.H.Hopkins, P.D.Carr, J.L.Khurana, J.G.Oakeshott, C.Scott, C.J.Jackson. Evolutionary Expansion of the Amidohydrolase Superfamily in Response to Synthetic Compounds: Molinate and Diuron Hydrolases. To Be Published.