Iron in PDB 6gpn: Crystal Structure of the Csid Glutarate Hydroxylase in Complex with N- Oxalylglycine

The structure of Crystal Structure of the Csid Glutarate Hydroxylase in Complex with N- Oxalylglycine, PDB code: 6gpn 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)	42.91 / 2.20
Space group	P 4 21 2
Cell size a, b, c (Å), α, β, γ (°)	121.380, 121.380, 136.570, 90.00, 90.00, 90.00
R / Rfree (%)	18.7 / 21.1

The binding sites of Iron atom in the Crystal Structure of the Csid Glutarate Hydroxylase in Complex with N- Oxalylglycine (pdb code 6gpn). 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 N- Oxalylglycine, PDB code: 6gpn:
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 N- Oxalylglycine


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 N- Oxalylglycine within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe401 b:66.7 occ:1.00 NE2 A:HIS292 2.4 43.3 1.0 NE2 A:HIS160 2.4 49.5 1.0 OD1 A:ASP162 2.4 55.7 1.0 O A:HOH594 2.8 49.4 1.0 CG A:ASP162 3.2 51.9 1.0 CE1 A:HIS160 3.3 45.0 1.0 OD2 A:ASP162 3.3 45.8 1.0 CD2 A:HIS292 3.3 41.8 1.0 O A:HOH580 3.3 58.1 1.0 CE1 A:HIS292 3.4 42.9 1.0 CD2 A:HIS160 3.5 48.1 1.0 ND1 A:HIS160 4.4 46.4 1.0 CG A:HIS292 4.5 41.7 1.0 ND1 A:HIS292 4.5 43.8 1.0 CG A:HIS160 4.5 48.4 1.0 CB A:ASP162 4.6 46.1 1.0 NH1 A:ARG311 4.7 69.7 1.0 SD A:MET175 4.9 79.0 1.0 CE A:MET157 5.0 90.4 1.0

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


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 N- Oxalylglycine within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe401 b:55.6 occ:1.00 NE2 B:HIS292 2.4 34.7 1.0 OD1 B:ASP162 2.4 47.1 1.0 NE2 B:HIS160 2.4 38.2 1.0 O2 B:OGA402 2.5 92.1 1.0 O2' B:OGA402 2.6 87.7 1.0 CD2 B:HIS292 3.1 32.0 1.0 CG B:ASP162 3.2 48.3 1.0 CE1 B:HIS160 3.2 35.7 1.0 C2 B:OGA402 3.3 95.1 1.0 C1 B:OGA402 3.3 94.8 1.0 OD2 B:ASP162 3.3 44.6 1.0 CD2 B:HIS160 3.4 39.3 1.0 CE1 B:HIS292 3.5 36.4 1.0 CG B:HIS292 4.3 37.1 1.0 ND1 B:HIS160 4.4 38.0 1.0 O B:HOH657 4.5 67.0 1.0 ND1 B:HIS292 4.5 38.3 1.0 CG B:HIS160 4.5 40.7 1.0 O1 B:OGA402 4.5 89.9 1.0 CB B:ASP162 4.6 39.0 1.0 N1 B:OGA402 4.6 97.4 1.0 NH1 B:ARG311 4.9 56.0 1.0 SD B:MET175 5.0 66.9 1.0 CA B:ASP162 5.0 34.6 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