Zinc in PDB 1r61: The Structure of Predicted Metal-Dependent Hydrolase From Bacillus Stearothermophilus

The structure of The Structure of Predicted Metal-Dependent Hydrolase From Bacillus Stearothermophilus, PDB code: 1r61 was solved by J.Maderova, D.Borek, D.Tomchick, A.Joachimiak, F.Collart, Z.Otwinowski, Midwest Center For Structural Genomics (Mcsg), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	35.00 / 2.50
Space group	P 41 21 2
Cell size a, b, c (Å), α, β, γ (°)	118.434, 118.434, 123.542, 90.00, 90.00, 90.00
R / Rfree (%)	17.6 / 21.5

The binding sites of Zinc atom in the The Structure of Predicted Metal-Dependent Hydrolase From Bacillus Stearothermophilus (pdb code 1r61). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 3 binding sites of Zinc where determined in the The Structure of Predicted Metal-Dependent Hydrolase From Bacillus Stearothermophilus, PDB code: 1r61:
Jump to Zinc binding site number: 1; 2; 3;

Zinc binding site 1 out of 3 in the The Structure of Predicted Metal-Dependent Hydrolase From Bacillus Stearothermophilus


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of The Structure of Predicted Metal-Dependent Hydrolase From Bacillus Stearothermophilus within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn1001 b:87.3 occ:0.50 OD2 A:ASP51 2.7 46.1 1.0 OE1 A:GLU167 2.7 53.9 1.0 NE2 A:HIS155 2.8 48.4 1.0 OE2 A:GLU167 3.0 47.6 1.0 CD A:GLU167 3.2 43.9 1.0 CD2 A:HIS155 3.5 41.2 1.0 CG A:ASP51 3.6 57.3 1.0 CB A:ASP51 3.7 41.0 1.0 CE1 A:HIS155 3.9 48.7 1.0 CG A:GLU167 4.6 46.5 1.0 ND1 A:HIS45 4.7 54.5 1.0 CE1 A:HIS45 4.7 52.7 1.0 NE2 A:HIS49 4.7 39.4 1.0 OD1 A:ASP51 4.7 61.0 1.0 CG A:HIS155 4.8 48.8 1.0 O A:HOH2103 4.9 60.9 1.0 ND1 A:HIS155 4.9 41.1 1.0 CG2 A:ILE165 5.0 41.6 1.0

Zinc binding site 2 out of 3 in the The Structure of Predicted Metal-Dependent Hydrolase From Bacillus Stearothermophilus


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of The Structure of Predicted Metal-Dependent Hydrolase From Bacillus Stearothermophilus within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn1002 b:92.8 occ:0.40 ZN B:ZN1002 0.0 92.8 0.4 OE2 B:GLU167 2.3 55.4 1.0 ZN B:ZN1002 2.5 94.3 0.4 OE1 B:GLU167 2.8 72.3 1.0 CD B:GLU167 2.8 61.2 1.0 NE2 B:HIS155 2.9 57.1 1.0 OD1 B:ASP51 3.1 83.5 1.0 O B:HOH2099 3.3 82.4 1.0 CE1 B:HIS155 3.5 62.7 1.0 CE1 B:HIS55 3.6 72.2 1.0 O B:HOH2061 3.8 80.9 1.0 ND1 B:HIS55 3.9 67.8 1.0 CG B:ASP51 4.0 70.0 1.0 CD2 B:HIS155 4.1 59.1 1.0 CG B:GLU167 4.3 47.8 1.0 OD2 B:ASP51 4.5 68.4 1.0 CA B:GLY144 4.5 44.7 1.0 NE2 B:HIS49 4.7 46.1 1.0 O B:LEU143 4.7 56.9 1.0 ND1 B:HIS45 4.7 42.5 1.0 N B:ILE145 4.7 51.8 1.0 NE2 B:HIS55 4.7 57.6 1.0 ND1 B:HIS155 4.8 65.1 1.0

Zinc binding site 3 out of 3 in the The Structure of Predicted Metal-Dependent Hydrolase From Bacillus Stearothermophilus


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of The Structure of Predicted Metal-Dependent Hydrolase From Bacillus Stearothermophilus within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn1002 b:94.3 occ:0.40 ZN B:ZN1002 0.0 94.3 0.4 ZN B:ZN1002 2.5 92.8 0.4 NE2 B:HIS49 2.6 46.1 1.0 ND1 B:HIS45 2.6 42.5 1.0 O B:HOH2099 2.9 82.4 1.0 OE1 B:GLU167 2.9 72.3 1.0 CD2 B:HIS49 3.4 54.2 1.0 CG B:HIS45 3.5 45.0 1.0 CB B:HIS45 3.6 47.5 1.0 CD B:GLU167 3.6 61.2 1.0 CE1 B:HIS45 3.7 46.8 1.0 CE1 B:HIS49 3.7 41.1 1.0 OD1 B:ASP51 3.8 83.5 1.0 OD2 B:ASP51 3.8 68.4 1.0 OE2 B:GLU167 3.9 55.4 1.0 CE1 B:HIS55 3.9 72.2 1.0 CG B:ASP51 4.0 70.0 1.0 O B:LEU143 4.2 56.9 1.0 ND1 B:HIS55 4.3 67.8 1.0 CA B:HIS45 4.5 44.4 1.0 NE2 B:HIS55 4.6 57.6 1.0 CG B:HIS49 4.6 50.4 1.0 CD2 B:HIS45 4.7 48.8 1.0 NE2 B:HIS45 4.7 38.7 1.0 ND1 B:HIS49 4.7 50.3 1.0 CG B:GLU167 4.8 47.8 1.0 O B:HIS45 4.9 56.0 1.0 CB B:GLU167 4.9 46.1 1.0 CB B:ASP51 5.0 64.7 1.0

J.Maderova, D.Borek, D.Tomchick, A.Joachimiak, F.Collart, Z.Otwinowski. The Structure of Potential Metal-Dependent Hydrolase with Cyclase Activity To Be Published.