Copper in PDB 4flm: S-Formylglutathione Hydrolase W197I Variant Containing Copper

All present enzymatic activity of S-Formylglutathione Hydrolase W197I Variant Containing Copper:
3.1.2.12;

The structure of S-Formylglutathione Hydrolase W197I Variant Containing Copper, PDB code: 4flm was solved by P.M.Legler, C.B.Millard, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	42.52 / 2.41
Space group	P 1
Cell size a, b, c (Å), α, β, γ (°)	48.826, 49.203, 66.845, 73.92, 80.44, 62.60
R / Rfree (%)	19.2 / 25

The binding sites of Copper atom in the S-Formylglutathione Hydrolase W197I Variant Containing Copper (pdb code 4flm). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total 2 binding sites of Copper where determined in the S-Formylglutathione Hydrolase W197I Variant Containing Copper, PDB code: 4flm:
Jump to Copper binding site number: 1; 2;

Copper binding site 1 out of 2 in the S-Formylglutathione Hydrolase W197I Variant Containing Copper


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of S-Formylglutathione Hydrolase W197I Variant Containing Copper within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu301 b:36.2 occ:0.40 ND1 A:HIS140 2.1 39.0 1.0 O A:HOH454 2.3 32.0 1.0 O A:MET1 2.4 41.6 1.0 CE1 A:HIS140 2.9 39.1 1.0 N A:MET1 3.1 40.9 1.0 CB A:MET1 3.1 40.8 1.0 C A:MET1 3.1 41.0 1.0 CG A:HIS140 3.2 38.0 1.0 CA A:MET1 3.2 40.1 1.0 CB A:HIS140 3.6 38.0 1.0 NE2 A:HIS140 4.1 38.2 1.0 CA A:HIS140 4.1 38.4 1.0 CD2 A:HIS140 4.2 37.6 1.0 N A:LYS2 4.3 39.9 1.0 CG A:MET1 4.4 40.8 1.0

Copper binding site 2 out of 2 in the S-Formylglutathione Hydrolase W197I Variant Containing Copper


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 2 of S-Formylglutathione Hydrolase W197I Variant Containing Copper within 5.0Å range: probe atom residue distance (Å) B Occ B:Cu301 b:31.1 occ:0.40 N B:MET1 1.9 30.8 1.0 ND1 B:HIS140 2.1 30.1 1.0 O B:HOH473 2.1 39.5 1.0 O B:MET1 2.6 31.1 1.0 CE1 B:HIS140 2.9 29.8 1.0 CA B:MET1 2.9 31.0 1.0 C B:MET1 3.2 31.2 1.0 CG B:HIS140 3.2 29.1 1.0 CB B:MET1 3.6 30.5 1.0 CB B:HIS140 3.6 28.7 1.0 CA B:HIS140 4.1 29.0 1.0 NE2 B:HIS140 4.1 29.0 1.0 CG B:MET1 4.2 30.1 1.0 CD2 B:HIS140 4.2 29.2 1.0 N B:LYS2 4.5 30.6 1.0 N B:HIS140 5.0 28.5 1.0

P.M.Legler, D.H.Leary, W.J.Hervey, C.B.Millard. A Role For His-160 in Peroxide Inhibition of S. Cerevisiae S-Formylglutathione Hydrolase: Evidence For An Oxidation Sensitive Motif. Arch.Biochem.Biophys. V. 528 7 2012.
ISSN: ISSN 0003-9861
PubMed: 22906720
DOI: 10.1016/J.ABB.2012.08.001