Iron in PDB 1za5: Q69H-Fesod

All present enzymatic activity of Q69H-Fesod:
1.15.1.1;

The structure of Q69H-Fesod, PDB code: 1za5 was solved by E.Yikilmaz, D.W.Rodgers, A.F.Miller, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	19.96 / 1.80
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	41.202, 84.921, 61.634, 90.00, 108.37, 90.00
R / Rfree (%)	19.9 / 23.7

The binding sites of Iron atom in the Q69H-Fesod (pdb code 1za5). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the Q69H-Fesod, PDB code: 1za5:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the Q69H-Fesod


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Q69H-Fesod within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe193 b:19.9 occ:1.00 OD1 A:ASP156 2.0 20.0 1.0 NE2 A:HIS73 2.2 18.7 1.0 O A:HOH196 2.2 15.1 1.0 NE2 A:HIS160 2.2 19.8 1.0 NE2 A:HIS26 2.2 15.8 1.0 CD2 A:HIS160 3.1 17.9 1.0 CE1 A:HIS73 3.1 21.7 1.0 CD2 A:HIS73 3.1 19.7 1.0 CG A:ASP156 3.1 21.9 1.0 CE1 A:HIS26 3.1 17.0 1.0 CD2 A:HIS26 3.2 17.9 1.0 CE1 A:HIS160 3.2 16.2 1.0 OD2 A:ASP156 3.6 20.5 1.0 ND1 A:HIS73 4.2 19.1 1.0 CG A:HIS73 4.2 19.8 1.0 ND1 A:HIS26 4.2 16.7 1.0 CG A:HIS160 4.3 18.2 1.0 ND1 A:HIS160 4.3 16.8 1.0 CG A:HIS26 4.3 16.2 1.0 CB A:ASP156 4.4 18.6 1.0 CZ2 A:TRP122 4.4 20.3 1.0 CH2 A:TRP122 4.4 21.2 1.0 CB A:TRP158 4.5 16.3 1.0 OH A:TYR34 4.6 29.5 1.0 CG A:TRP158 4.7 18.3 1.0 CB A:ALA161 4.9 18.2 1.0

Iron binding site 2 out of 2 in the Q69H-Fesod


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Q69H-Fesod within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe393 b:18.2 occ:1.00 OD1 B:ASP356 1.9 15.7 1.0 NE2 B:HIS360 2.1 16.3 1.0 NE2 B:HIS273 2.1 19.1 1.0 NE2 B:HIS226 2.2 16.9 1.0 O B:HOH394 2.2 17.4 1.0 CE1 B:HIS226 3.0 16.8 1.0 CG B:ASP356 3.0 16.9 1.0 CE1 B:HIS360 3.1 17.4 1.0 CD2 B:HIS360 3.1 17.4 1.0 CD2 B:HIS273 3.1 17.9 1.0 CE1 B:HIS273 3.1 18.9 1.0 CD2 B:HIS226 3.2 17.1 1.0 OD2 B:ASP356 3.5 17.3 1.0 ND1 B:HIS360 4.2 16.2 1.0 ND1 B:HIS226 4.2 18.4 1.0 ND1 B:HIS273 4.2 18.8 1.0 CG B:HIS273 4.2 19.4 1.0 CG B:HIS360 4.2 15.8 1.0 CG B:HIS226 4.3 16.6 1.0 CB B:ASP356 4.3 15.4 1.0 CH2 B:TRP322 4.4 19.2 1.0 CZ2 B:TRP322 4.4 18.8 1.0 CB B:TRP358 4.5 14.7 1.0 OH B:TYR234 4.6 26.1 1.0 CG B:TRP358 4.7 15.3 1.0 CB B:ALA361 4.8 17.7 1.0

E.Yikilmaz, D.W.Rodgers, A.F.Miller. The Crucial Importance of Chemistry in the Structure-Function Link: Manipulating Hydrogen Bonding in Iron-Containing Superoxide Dismutase. Biochemistry V. 45 1151 2006.
ISSN: ISSN 0006-2960
PubMed: 16430211
DOI: 10.1021/BI051495D