Iron in PDB 6gkc: 2 Minute FE2+ Soak Structure of Synftn

All present enzymatic activity of 2 Minute FE2+ Soak Structure of Synftn:
1.16.3.2;

The structure of 2 Minute FE2+ Soak Structure of Synftn, PDB code: 6gkc was solved by A.M.Hemmings, J.M.Bradley, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	53.41 / 1.97
Space group	F 4 3 2
Cell size a, b, c (Å), α, β, γ (°)	177.157, 177.157, 177.157, 90.00, 90.00, 90.00
R / Rfree (%)	17.8 / 20.1

The binding sites of Iron atom in the 2 Minute FE2+ Soak Structure of Synftn (pdb code 6gkc). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the 2 Minute FE2+ Soak Structure of Synftn, PDB code: 6gkc:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the 2 Minute FE2+ Soak Structure of Synftn


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of 2 Minute FE2+ Soak Structure of Synftn within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe201 b:41.8 occ:0.50 OE1 A:GLU33 2.1 38.7 1.0 OE2 A:GLU66 2.1 36.5 1.0 O A:HOH305 2.3 56.9 1.0 ND1 A:HIS69 2.6 33.9 1.0 O A:HOH304 2.6 48.7 1.0 CD A:GLU66 2.8 35.9 1.0 OE1 A:GLU66 3.0 41.5 1.0 CD A:GLU33 3.0 39.6 1.0 OE2 A:GLU33 3.3 40.1 1.0 CG A:HIS69 3.5 34.8 1.0 CE1 A:HIS69 3.5 36.0 1.0 CB A:HIS69 3.7 30.1 1.0 CG2 A:THR113 3.8 30.6 0.8 FE A:FE202 3.9 48.2 0.6 OE1 A:GLN143 4.1 36.0 1.0 O A:HOH395 4.2 43.7 1.0 CG A:GLU66 4.2 34.1 1.0 O A:HOH378 4.2 45.5 1.0 CA A:GLU66 4.4 28.1 1.0 CG A:GLU33 4.4 36.0 1.0 O A:HOH340 4.5 55.9 1.0 CB A:GLU66 4.5 30.2 1.0 NE2 A:HIS69 4.7 33.8 1.0 CD2 A:HIS69 4.7 33.4 1.0 CB A:GLU33 4.7 32.3 1.0 O A:HOH382 4.8 35.4 1.0 O A:GLU66 4.8 29.2 1.0 CD A:GLN143 4.9 35.6 1.0 CB A:THR113 4.9 33.7 0.2 CB A:THR113 4.9 33.9 0.8 CG2 A:THR113 5.0 34.9 0.2

Iron binding site 2 out of 2 in the 2 Minute FE2+ Soak Structure of Synftn


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of 2 Minute FE2+ Soak Structure of Synftn within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe202 b:48.2 occ:0.56 OE1 A:GLU66 2.0 41.5 1.0 O A:HOH304 2.1 48.7 1.0 O A:HOH309 2.3 69.2 1.0 OE2 A:GLU110 2.3 44.0 1.0 OE1 A:GLU110 2.5 38.2 1.0 CD A:GLU110 2.7 39.8 1.0 O A:HOH340 3.0 55.9 1.0 CD A:GLU66 3.3 35.9 1.0 O A:HOH378 3.4 45.5 1.0 OE1 A:GLN143 3.9 36.0 1.0 FE A:FE201 3.9 41.8 0.5 OG A:SER146 3.9 41.0 1.0 OE2 A:GLU66 4.0 36.5 1.0 CB A:SER146 4.2 33.2 1.0 CG A:GLU110 4.2 41.3 1.0 CG A:GLU66 4.3 34.1 1.0 CE1 A:HIS69 4.3 36.0 1.0 OE1 A:GLU62 4.5 36.5 1.0 ND1 A:HIS69 4.6 33.9 1.0 O A:HOH306 4.6 40.8 1.0 NE2 A:GLN143 4.7 32.9 1.0 CD A:GLN143 4.7 35.6 1.0 CE2 A:TYR40 4.7 28.7 1.0 OH A:TYR40 4.7 35.9 1.0

J.M.Bradley, D.A.Svistunenko, J.Pullin, N.Hill, R.K.Stuart, B.Palenik, M.T.Wilson, A.M.Hemmings, G.R.Moore, N.E.Le Brun. Reaction of O2WITH A Diiron Protein Generates A Mixed-Valent FE2+/FE3+Center and Peroxide. Proc. Natl. Acad. Sci. V. 116 2058 2019U.S.A..
ISSN: ESSN 1091-6490
PubMed: 30659147
DOI: 10.1073/PNAS.1809913116