Iron in PDB 6hl8: Crystal Structure of the Csid Glutarate Hydroxylase in Complex with Glutarate

The structure of Crystal Structure of the Csid Glutarate Hydroxylase in Complex with Glutarate, PDB code: 6hl8 was solved by R.M.Williams, O.Mayans, J.S.Hartig, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	29.70 / 2.40
Space group	P 4 21 2
Cell size a, b, c (Å), α, β, γ (°)	120.800, 120.800, 136.430, 90.00, 90.00, 90.00
R / Rfree (%)	17.5 / 22

The binding sites of Iron atom in the Crystal Structure of the Csid Glutarate Hydroxylase in Complex with Glutarate (pdb code 6hl8). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the Crystal Structure of the Csid Glutarate Hydroxylase in Complex with Glutarate, PDB code: 6hl8:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the Crystal Structure of the Csid Glutarate Hydroxylase in Complex with Glutarate


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Crystal Structure of the Csid Glutarate Hydroxylase in Complex with Glutarate within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe401 b:45.6 occ:1.00 NE2 A:HIS292 2.3 43.8 1.0 OD1 A:ASP162 2.3 44.0 1.0 NE2 A:HIS160 2.4 43.6 1.0 O A:HOH611 2.7 50.3 1.0 O3 A:GUA402 2.9 80.8 1.0 CG A:ASP162 3.1 42.4 1.0 OD2 A:ASP162 3.1 44.6 1.0 CD2 A:HIS292 3.2 39.0 1.0 CE1 A:HIS292 3.2 41.3 1.0 CD2 A:HIS160 3.3 41.2 1.0 CE1 A:HIS160 3.3 43.1 1.0 C5 A:GUA402 3.9 84.3 1.0 ND1 A:HIS292 4.3 42.5 1.0 CG A:HIS292 4.3 41.5 1.0 ND1 A:HIS160 4.4 41.3 1.0 C3 A:GUA402 4.4 79.4 1.0 CG A:HIS160 4.4 42.2 1.0 CB A:ASP162 4.5 33.8 1.0 O4 A:GUA402 4.7 89.8 1.0 C4 A:GUA402 4.7 81.0 1.0 SD A:MET175 4.8 77.2 1.0 O2 A:GUA402 4.8 94.5 1.0 CA A:ASP162 5.0 37.9 1.0

Iron binding site 2 out of 2 in the Crystal Structure of the Csid Glutarate Hydroxylase in Complex with Glutarate


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Crystal Structure of the Csid Glutarate Hydroxylase in Complex with Glutarate within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe401 b:47.5 occ:1.00 OD1 B:ASP162 2.3 44.7 1.0 NE2 B:HIS292 2.3 38.9 1.0 NE2 B:HIS160 2.3 43.0 1.0 O B:HOH649 2.5 60.9 1.0 O4 B:GUA402 2.8 84.4 1.0 CG B:ASP162 3.1 37.9 1.0 OD2 B:ASP162 3.1 40.3 1.0 CE1 B:HIS292 3.2 32.2 1.0 CE1 B:HIS160 3.3 39.2 1.0 CD2 B:HIS292 3.3 32.8 1.0 CD2 B:HIS160 3.3 38.2 1.0 C5 B:GUA402 3.9 81.6 1.0 C3 B:GUA402 4.1 74.4 1.0 ND1 B:HIS292 4.3 37.1 1.0 CG B:HIS292 4.4 37.2 1.0 ND1 B:HIS160 4.4 38.8 1.0 CG B:HIS160 4.4 41.4 1.0 CB B:ASP162 4.5 29.7 1.0 C4 B:GUA402 4.7 77.6 1.0 O3 B:GUA402 4.8 84.2 1.0 CA B:ASP162 5.0 29.2 1.0

S.Knorr, M.Sinn, D.Galetskiy, R.M.Williams, C.Wang, N.Muller, O.Mayans, D.Schleheck, J.S.Hartig. Widespread Bacterial Lysine Degradation Proceeding Via Glutarate and L-2-Hydroxyglutarate. Nat Commun V. 9 5071 2018.
ISSN: ESSN 2041-1723
PubMed: 30498244
DOI: 10.1038/S41467-018-07563-6