Iron in PDB 5lx4: Cys-Gly Dipeptidase Glij Mutant D38H

All present enzymatic activity of Cys-Gly Dipeptidase Glij Mutant D38H:
3.4.13.19;

The structure of Cys-Gly Dipeptidase Glij Mutant D38H, PDB code: 5lx4 was solved by E.M.Huber, M.Groll, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	15.00 / 1.90
Space group	P 32 2 1
Cell size a, b, c (Å), α, β, γ (°)	98.970, 98.970, 106.050, 90.00, 90.00, 120.00
R / Rfree (%)	16.3 / 19

The binding sites of Iron atom in the Cys-Gly Dipeptidase Glij Mutant D38H (pdb code 5lx4). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total only one binding site of Iron was determined in the Cys-Gly Dipeptidase Glij Mutant D38H, PDB code: 5lx4:

Iron binding site 1 out of 1 in the Cys-Gly Dipeptidase Glij Mutant D38H


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Cys-Gly Dipeptidase Glij Mutant D38H within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe401 b:80.2 occ:0.75 OE2 A:GLU134 2.0 54.6 1.0 O A:HOH696 2.6 45.3 1.0 NE2 A:HIS224 2.7 32.4 1.0 NE2 A:HIS203 2.8 55.1 0.8 CD A:GLU134 3.0 50.9 1.0 CD2 A:HIS203 3.4 51.6 0.8 CE1 A:HIS224 3.5 32.2 1.0 OE1 A:GLU134 3.5 51.4 1.0 NE2 A:HIS161 3.6 54.9 0.8 CD2 A:HIS224 3.6 26.0 1.0 CD2 A:HIS161 3.7 56.2 0.8 CE1 A:HIS203 3.8 54.5 0.8 CE1 A:HIS25 3.8 37.5 1.0 NE2 A:HIS23 3.8 34.7 1.0 OD1 A:ASP294 4.1 34.4 1.0 OD2 A:ASP294 4.2 35.1 1.0 CG A:GLU134 4.3 48.5 1.0 CD2 A:HIS23 4.3 33.2 1.0 NE2 A:HIS25 4.3 37.8 1.0 CG A:ASP294 4.4 32.9 1.0 CG A:HIS203 4.5 47.8 0.8 ND1 A:HIS224 4.6 30.9 1.0 CE1 A:HIS23 4.6 34.4 1.0 ND1 A:HIS203 4.7 51.7 0.8 CG A:HIS224 4.7 29.6 1.0 NH1 A:ARG235 4.9 48.5 1.0 CE1 A:HIS161 4.9 56.5 0.8 ND1 A:HIS25 4.9 36.0 1.0

A.Marion, M.Groll, D.H.Scharf, K.Scherlach, M.Glaser, H.Sievers, M.Schuster, C.Hertweck, A.A.Brakhage, I.Antes, E.M.Huber. Gliotoxin Biosynthesis: Structure, Mechanism, and Metal Promiscuity of Carboxypeptidase Glij. Acs Chem. Biol. V. 12 1874 2017.
ISSN: ESSN 1554-8937
PubMed: 28525266
DOI: 10.1021/ACSCHEMBIO.6B00847