Cobalt in PDB 4az4: E.Coli Deformylase with Co(II) and Hydrosulfide

All present enzymatic activity of E.Coli Deformylase with Co(II) and Hydrosulfide:
3.5.1.88;

The structure of E.Coli Deformylase with Co(II) and Hydrosulfide, PDB code: 4az4 was solved by G.J.Palm, W.Hinrichs, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	46.38 / 1.80
Space group	P 61 2 2
Cell size a, b, c (Å), α, β, γ (°)	54.631, 54.631, 229.416, 90.00, 90.00, 120.00
R / Rfree (%)	18.9 / 22.1

The binding sites of Cobalt atom in the E.Coli Deformylase with Co(II) and Hydrosulfide (pdb code 4az4). This binding sites where shown within 5.0 Angstroms radius around Cobalt atom.
In total only one binding site of Cobalt was determined in the E.Coli Deformylase with Co(II) and Hydrosulfide, PDB code: 4az4:

Cobalt binding site 1 out of 1 in the E.Coli Deformylase with Co(II) and Hydrosulfide


Mono view


Stereo pair view

A full contact list of Cobalt with other atoms in the Co binding site number 1 of E.Coli Deformylase with Co(II) and Hydrosulfide within 5.0Å range: probe atom residue distance (Å) B Occ A:Co1164 b:33.4 occ:1.00 NE2 A:HIS132 2.0 29.5 1.0 NE2 A:HIS136 2.1 36.0 1.0 SG A:CYS90 2.3 37.1 1.0 S A:H2S1165 2.3 45.0 0.7 O A:HOH2025 2.4 24.4 0.3 CD2 A:HIS132 3.0 28.0 1.0 O A:HOH2024 3.0 39.1 0.3 CE1 A:HIS136 3.1 37.3 1.0 CD2 A:HIS136 3.1 33.7 1.0 CE1 A:HIS132 3.1 29.2 1.0 CB A:CYS90 3.2 36.9 1.0 O A:HOH2057 3.6 33.9 1.0 NE2 A:GLN50 3.6 41.2 1.0 CA A:CYS90 3.6 36.9 1.0 CD A:GLN50 4.1 39.9 1.0 CG A:HIS132 4.2 26.7 1.0 ND1 A:HIS132 4.2 26.8 1.0 ND1 A:HIS136 4.2 37.5 1.0 N A:LEU91 4.2 41.0 1.0 OE1 A:GLN50 4.2 38.1 1.0 CG A:HIS136 4.2 35.1 1.0 C A:CYS90 4.4 40.3 1.0 O A:HOH2077 4.5 31.2 1.0 OE2 A:GLU133 4.6 31.8 1.0 O A:GLY89 4.6 33.4 1.0 OE1 A:GLU133 4.8 32.2 1.0 N A:CYS90 4.9 37.1 1.0 N A:SER92 5.0 46.0 1.0 O A:HOH2058 5.0 49.6 1.0

M.Strianese, G.J.Palm, S.Milione, O.Kuhl, W.Hinrichs, C.Pellecchia. A Fret Enzyme-Based Probe For Monitoring Hydrogen Sulfide. Inorg.Chem. V. 51 11220 2012.
ISSN: ISSN 0020-1669
PubMed: 23072298
DOI: 10.1021/IC301363D