Nickel in PDB 1ws0: Structure Analysis of Peptide Deformylase From Bacillus Cereus

All present enzymatic activity of Structure Analysis of Peptide Deformylase From Bacillus Cereus:
3.5.1.88;

The structure of Structure Analysis of Peptide Deformylase From Bacillus Cereus, PDB code: 1ws0 was solved by J.H.Moon, J.K.Park, E.E.Kim, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	24.92 / 1.70
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	44.330, 42.802, 84.806, 90.00, 90.00, 90.00
R / Rfree (%)	20 / 22.3

The binding sites of Nickel atom in the Structure Analysis of Peptide Deformylase From Bacillus Cereus (pdb code 1ws0). This binding sites where shown within 5.0 Angstroms radius around Nickel atom.
In total only one binding site of Nickel was determined in the Structure Analysis of Peptide Deformylase From Bacillus Cereus, PDB code: 1ws0:

Nickel binding site 1 out of 1 in the Structure Analysis of Peptide Deformylase From Bacillus Cereus


Mono view


Stereo pair view

A full contact list of Nickel with other atoms in the Ni binding site number 1 of Structure Analysis of Peptide Deformylase From Bacillus Cereus within 5.0Å range: probe atom residue distance (Å) B Occ A:Ni200 b:11.9 occ:1.00 NE2 A:HIS132 2.0 10.7 1.0 NE2 A:HIS136 2.1 10.9 1.0 O A:HOH202 2.1 14.6 1.0 SG A:CYS90 2.2 11.9 1.0 CD2 A:HIS132 2.9 11.2 1.0 CD2 A:HIS136 3.0 10.3 1.0 CE1 A:HIS136 3.1 11.2 1.0 CE1 A:HIS132 3.1 10.3 1.0 CB A:CYS90 3.3 11.8 1.0 O A:HOH205 3.6 13.7 1.0 NE2 A:GLN51 3.7 11.8 1.0 O A:HOH212 3.7 19.8 1.0 OE1 A:GLN51 3.8 12.8 1.0 CA A:CYS90 3.9 14.8 1.0 CD A:GLN51 3.9 11.5 1.0 OE2 A:GLU133 4.0 13.8 1.0 CG A:HIS132 4.1 9.8 1.0 ND1 A:HIS132 4.2 12.6 1.0 CG A:HIS136 4.2 11.8 1.0 ND1 A:HIS136 4.2 13.2 1.0 OE1 A:GLU133 4.5 15.2 1.0 O A:HOH203 4.5 11.4 1.0 N A:LEU91 4.6 14.6 1.0 CD A:GLU133 4.6 11.3 1.0 C A:CYS90 4.6 16.6 1.0 O A:GLY89 4.8 19.0 1.0

J.H.Moon, J.K.Park, E.E.Kim. Structure Analysis of Peptide Deformylase From Bacillus Cereus Proteins V. 61 217 2005.
ISSN: ISSN 0887-3585
PubMed: 16049914
DOI: 10.1002/PROT.20526