Iron in PDB 1isa: Structure-Function in E. Coli Iron Superoxide Dismutase: Comparisons with the Manganese Enzyme From T. Thermophilus

All present enzymatic activity of Structure-Function in E. Coli Iron Superoxide Dismutase: Comparisons with the Manganese Enzyme From T. Thermophilus:
1.15.1.1;

The structure of Structure-Function in E. Coli Iron Superoxide Dismutase: Comparisons with the Manganese Enzyme From T. Thermophilus, PDB code: 1isa was solved by M.S.Lah, M.Dixon, K.A.Pattridge, W.C.Stallings, J.A.Fee, M.L.Ludwig, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	40.00 / 1.80
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	81.550, 75.080, 71.530, 90.00, 90.00, 90.00
R / Rfree (%)	18.8 / n/a

The binding sites of Iron atom in the Structure-Function in E. Coli Iron Superoxide Dismutase: Comparisons with the Manganese Enzyme From T. Thermophilus (pdb code 1isa). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the Structure-Function in E. Coli Iron Superoxide Dismutase: Comparisons with the Manganese Enzyme From T. Thermophilus, PDB code: 1isa:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the Structure-Function in E. Coli Iron Superoxide Dismutase: Comparisons with the Manganese Enzyme From T. Thermophilus


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Structure-Function in E. Coli Iron Superoxide Dismutase: Comparisons with the Manganese Enzyme From T. Thermophilus within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe193 b:4.3 occ:1.00 OD2 A:ASP156 2.0 4.4 1.0 O A:HOH194 2.0 6.8 1.0 NE2 A:HIS73 2.1 4.0 1.0 NE2 A:HIS160 2.1 5.6 1.0 NE2 A:HIS26 2.2 4.6 1.0 CD2 A:HIS73 3.0 3.2 1.0 CD2 A:HIS160 3.0 4.2 1.0 CE1 A:HIS73 3.0 4.1 1.0 CG A:ASP156 3.0 3.8 1.0 CD2 A:HIS26 3.1 2.7 1.0 CE1 A:HIS160 3.1 4.2 1.0 CE1 A:HIS26 3.2 2.0 1.0 OD1 A:ASP156 3.5 2.0 1.0 ND1 A:HIS73 4.1 2.0 1.0 CG A:HIS73 4.1 3.0 1.0 CG A:HIS160 4.2 4.7 1.0 ND1 A:HIS160 4.2 4.6 1.0 CG A:HIS26 4.2 3.1 1.0 ND1 A:HIS26 4.2 3.0 1.0 CB A:ASP156 4.3 3.7 1.0 CH2 A:TRP122 4.3 2.0 1.0 CZ2 A:TRP122 4.5 3.1 1.0 CB A:TRP158 4.6 3.2 1.0 CG A:TRP158 4.8 4.9 1.0 CB A:ALA161 5.0 2.3 1.0

Iron binding site 2 out of 2 in the Structure-Function in E. Coli Iron Superoxide Dismutase: Comparisons with the Manganese Enzyme From T. Thermophilus


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Structure-Function in E. Coli Iron Superoxide Dismutase: Comparisons with the Manganese Enzyme From T. Thermophilus within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe193 b:5.5 occ:1.00 OD2 B:ASP156 1.9 5.6 1.0 NE2 B:HIS73 2.0 4.8 1.0 O B:HOH194 2.1 8.1 1.0 NE2 B:HIS160 2.1 5.1 1.0 NE2 B:HIS26 2.2 6.8 1.0 CD2 B:HIS73 2.9 2.9 1.0 CG B:ASP156 3.0 4.1 1.0 CD2 B:HIS160 3.0 3.7 1.0 CE1 B:HIS73 3.0 4.9 1.0 CE1 B:HIS160 3.1 5.5 1.0 CD2 B:HIS26 3.1 4.4 1.0 CE1 B:HIS26 3.1 3.1 1.0 OD1 B:ASP156 3.4 3.8 1.0 CG B:HIS73 4.1 3.6 1.0 ND1 B:HIS73 4.1 4.2 1.0 CG B:HIS160 4.2 3.9 1.0 ND1 B:HIS160 4.2 4.6 1.0 ND1 B:HIS26 4.2 3.9 1.0 CG B:HIS26 4.2 4.0 1.0 CB B:ASP156 4.3 3.2 1.0 CH2 B:TRP122 4.4 3.1 1.0 CZ2 B:TRP122 4.5 4.6 1.0 CB B:TRP158 4.5 2.0 1.0 CG B:TRP158 4.7 2.3 1.0

M.S.Lah, M.M.Dixon, K.A.Pattridge, W.C.Stallings, J.A.Fee, M.L.Ludwig. Structure-Function in Escherichia Coli Iron Superoxide Dismutase: Comparisons with the Manganese Enzyme From Thermus Thermophilus. Biochemistry V. 34 1646 1995.
ISSN: ISSN 0006-2960
PubMed: 7849024
DOI: 10.1021/BI00005A021