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

Enzymatic activity of 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;

Protein crystallography data

The structure of Structure-Function in E. Coli Iron Superoxide Dismutase: Comparisons with the Manganese Enzyme From T. Thermophilus, PDB code: 1isc 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 (°) 81.610, 75.160, 71.580, 90.00, 90.00, 90.00
R / Rfree (%) 18.5 / n/a

Iron Binding Sites:

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 1isc). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 4 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: 1isc:
Jump to Iron binding site number: 1; 2; 3; 4;

Iron binding site 1 out of 4 in 1isc

Go back to Iron Binding Sites List in 1isc
Iron binding site 1 out of 4 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:6.2
occ:0.48
 FE A:FE193 0.0 6.2 0.5
FE A:FE193 0.1 7.7 0.5
O A:HOH196 1.9 8.7 0.5
NE2 A:HIS73 2.0 7.0 0.5
NE2 A:HIS160 2.0 6.9 0.5
O A:HOH196 2.0 6.4 0.5
OD2 A:ASP156 2.0 6.1 0.5
OD2 A:ASP156 2.1 7.3 0.5
N1 A:AZI195 2.1 7.1 0.5
NE2 A:HIS73 2.1 5.3 0.5
NE2 A:HIS160 2.1 5.0 0.5
NE2 A:HIS26 2.2 6.0 0.5
NE2 A:HIS26 2.2 5.3 0.5
N2 A:AZI195 2.8 8.0 0.5
CD2 A:HIS73 2.9 5.8 0.5
CE1 A:HIS73 2.9 6.7 0.5
CE1 A:HIS160 3.0 6.2 0.5
CD2 A:HIS160 3.0 5.4 0.5
CD2 A:HIS73 3.0 4.8 0.5
CD2 A:HIS26 3.1 4.2 0.5
CE1 A:HIS160 3.1 4.6 0.5
CD2 A:HIS26 3.1 3.8 0.5
CD2 A:HIS160 3.1 4.2 0.5
CE1 A:HIS73 3.1 4.2 0.5
CG A:ASP156 3.1 5.0 0.5
CG A:ASP156 3.1 5.6 0.5
CE1 A:HIS26 3.1 5.6 0.5
CE1 A:HIS26 3.2 5.1 0.5
OD1 A:ASP156 3.5 4.7 0.5
OD1 A:ASP156 3.6 4.2 0.5
N3 A:AZI195 3.7 5.8 0.5
ND1 A:HIS73 4.0 6.6 0.5
ND1 A:HIS160 4.1 6.0 0.5
CG A:HIS73 4.1 6.7 0.5
CG A:HIS160 4.1 6.5 0.5
CG A:HIS73 4.2 5.9 0.5
ND1 A:HIS73 4.2 5.3 0.5
ND1 A:HIS160 4.2 4.4 0.5
CG A:HIS26 4.2 3.9 0.5
CG A:HIS160 4.2 5.3 0.5
ND1 A:HIS26 4.2 5.6 0.5
CG A:HIS26 4.3 3.6 0.5
ND1 A:HIS26 4.3 5.1 0.5
CB A:ASP156 4.4 5.0 0.5
CB A:ASP156 4.4 5.4 0.5
CH2 A:TRP122 4.6 4.7 1.0
CZ2 A:TRP122 4.6 5.5 1.0
CB A:TRP158 4.7 2.6 1.0
CG A:TRP158 4.8 5.9 1.0

Iron binding site 2 out of 4 in 1isc

Go back to Iron Binding Sites List in 1isc
Iron binding site 2 out of 4 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
A:Fe193

b:7.7
occ:0.51
 FE A:FE193 0.0 7.7 0.5
FE A:FE193 0.1 6.2 0.5
OD2 A:ASP156 1.9 6.1 0.5
OD2 A:ASP156 1.9 7.3 0.5
O A:HOH196 2.0 8.7 0.5
NE2 A:HIS73 2.0 7.0 0.5
O A:HOH196 2.0 6.4 0.5
NE2 A:HIS160 2.1 6.9 0.5
NE2 A:HIS26 2.1 6.0 0.5
NE2 A:HIS73 2.1 5.3 0.5
NE2 A:HIS26 2.2 5.3 0.5
NE2 A:HIS160 2.2 5.0 0.5
N1 A:AZI195 2.2 7.1 0.5
N2 A:AZI195 2.9 8.0 0.5
CD2 A:HIS73 2.9 5.8 0.5
CD2 A:HIS160 3.0 5.4 0.5
CG A:ASP156 3.0 5.0 0.5
CD2 A:HIS73 3.0 4.8 0.5
CG A:ASP156 3.0 5.6 0.5
CE1 A:HIS73 3.0 6.7 0.5
CE1 A:HIS160 3.0 6.2 0.5
CE1 A:HIS26 3.1 5.6 0.5
CD2 A:HIS26 3.1 4.2 0.5
CE1 A:HIS26 3.1 5.1 0.5
CD2 A:HIS26 3.1 3.8 0.5
CD2 A:HIS160 3.1 4.2 0.5
CE1 A:HIS73 3.1 4.2 0.5
CE1 A:HIS160 3.2 4.6 0.5
OD1 A:ASP156 3.4 4.7 0.5
OD1 A:ASP156 3.5 4.2 0.5
N3 A:AZI195 3.8 5.8 0.5
ND1 A:HIS73 4.1 6.6 0.5
CG A:HIS73 4.1 6.7 0.5
ND1 A:HIS160 4.1 6.0 0.5
CG A:HIS160 4.2 6.5 0.5
CG A:HIS73 4.2 5.9 0.5
ND1 A:HIS26 4.2 5.6 0.5
ND1 A:HIS73 4.2 5.3 0.5
ND1 A:HIS26 4.2 5.1 0.5
CG A:HIS26 4.2 3.9 0.5
CB A:ASP156 4.2 5.0 0.5
CG A:HIS26 4.2 3.6 0.5
ND1 A:HIS160 4.3 4.4 0.5
CB A:ASP156 4.3 5.4 0.5
CG A:HIS160 4.3 5.3 0.5
CH2 A:TRP122 4.5 4.7 1.0
CZ2 A:TRP122 4.6 5.5 1.0
CB A:TRP158 4.7 2.6 1.0
CG A:TRP158 4.8 5.9 1.0

Iron binding site 3 out of 4 in 1isc

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Iron binding site 3 out of 4 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 3 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:6.2
occ:0.50
 FE B:FE193 0.0 6.2 0.5
FE B:FE193 0.3 10.9 0.5
NE2 B:HIS73 1.9 9.7 0.5
O B:HOH196 1.9 14.8 0.5
O B:HOH196 2.0 4.6 0.5
NE2 B:HIS160 2.0 11.0 0.5
OD2 B:ASP156 2.0 5.9 0.5
NE2 B:HIS73 2.1 4.5 0.5
NE2 B:HIS160 2.2 5.3 0.5
N1 B:AZI195 2.2 5.8 0.5
OD2 B:ASP156 2.2 11.1 0.5
NE2 B:HIS26 2.2 5.1 0.5
NE2 B:HIS26 2.3 9.7 0.5
CE1 B:HIS73 2.8 9.1 0.5
N2 B:AZI195 2.9 4.7 0.5
CE1 B:HIS160 2.9 10.6 0.5
CD2 B:HIS73 2.9 8.1 0.5
CE1 B:HIS73 3.0 4.1 0.5
CD2 B:HIS160 3.0 7.7 0.5
CE1 B:HIS160 3.0 6.1 0.5
CG B:ASP156 3.1 7.5 0.5
CD2 B:HIS73 3.1 3.2 0.5
CD2 B:HIS160 3.2 2.8 0.5
CD2 B:HIS26 3.2 3.6 0.5
CE1 B:HIS26 3.2 3.6 0.5
CD2 B:HIS26 3.2 6.2 0.5
CG B:ASP156 3.2 9.7 0.5
CE1 B:HIS26 3.3 6.5 0.5
OD1 B:ASP156 3.5 5.8 0.5
OD1 B:ASP156 3.6 6.6 0.5
N3 B:AZI195 3.8 4.3 0.5
ND1 B:HIS73 3.9 8.6 0.5
CG B:HIS73 4.0 7.4 0.5
ND1 B:HIS160 4.0 10.0 0.5
CG B:HIS160 4.1 8.5 0.5
ND1 B:HIS73 4.1 4.7 0.5
ND1 B:HIS160 4.2 5.0 0.5
CG B:HIS73 4.2 4.4 0.5
CG B:HIS160 4.3 4.8 0.5
ND1 B:HIS26 4.3 3.6 0.5
CG B:HIS26 4.3 3.7 0.5
CG B:HIS26 4.3 5.9 0.5
ND1 B:HIS26 4.4 6.1 0.5
CB B:ASP156 4.4 6.4 0.5
CB B:ASP156 4.5 7.9 0.5
CH2 B:TRP122 4.6 6.2 1.0
CZ2 B:TRP122 4.6 7.4 1.0
CB B:TRP158 4.6 2.0 1.0
CG B:TRP158 4.7 5.0 1.0
O B:HOH307 4.8 36.3 1.0
NE2 B:GLN69 4.9 8.9 1.0
CD1 B:TRP158 4.9 5.3 1.0

Iron binding site 4 out of 4 in 1isc

Go back to Iron Binding Sites List in 1isc
Iron binding site 4 out of 4 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 4 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:10.9
occ:0.53
 FE B:FE193 0.0 10.9 0.5
FE B:FE193 0.3 6.2 0.5
OD2 B:ASP156 1.8 5.9 0.5
NE2 B:HIS73 2.0 9.7 0.5
OD2 B:ASP156 2.0 11.1 0.5
O B:HOH196 2.0 14.8 0.5
NE2 B:HIS160 2.0 11.0 0.5
NE2 B:HIS26 2.1 5.1 0.5
NE2 B:HIS26 2.2 9.7 0.5
O B:HOH196 2.2 4.6 0.5
NE2 B:HIS160 2.2 5.3 0.5
NE2 B:HIS73 2.2 4.5 0.5
N1 B:AZI195 2.4 5.8 0.5
CD2 B:HIS73 2.9 8.1 0.5
CE1 B:HIS26 2.9 3.6 0.5
CG B:ASP156 2.9 7.5 0.5
CD2 B:HIS160 3.0 7.7 0.5
CE1 B:HIS73 3.0 9.1 0.5
CE1 B:HIS160 3.0 10.6 0.5
N2 B:AZI195 3.0 4.7 0.5
CD2 B:HIS26 3.1 3.6 0.5
CG B:ASP156 3.1 9.7 0.5
CE1 B:HIS26 3.1 6.5 0.5
CD2 B:HIS26 3.1 6.2 0.5
CD2 B:HIS160 3.1 2.8 0.5
CD2 B:HIS73 3.1 3.2 0.5
CE1 B:HIS160 3.1 6.1 0.5
CE1 B:HIS73 3.2 4.1 0.5
OD1 B:ASP156 3.4 5.8 0.5
OD1 B:ASP156 3.5 6.6 0.5
N3 B:AZI195 3.9 4.3 0.5
ND1 B:HIS26 4.1 3.6 0.5
CG B:HIS73 4.1 7.4 0.5
ND1 B:HIS73 4.1 8.6 0.5
ND1 B:HIS160 4.1 10.0 0.5
CG B:HIS160 4.1 8.5 0.5
CG B:HIS26 4.1 3.7 0.5
ND1 B:HIS26 4.2 6.1 0.5
CG B:HIS26 4.2 5.9 0.5
CB B:ASP156 4.2 6.4 0.5
ND1 B:HIS160 4.2 5.0 0.5
ND1 B:HIS73 4.3 4.7 0.5
CG B:HIS160 4.3 4.8 0.5
CG B:HIS73 4.3 4.4 0.5
CB B:ASP156 4.3 7.9 0.5
CH2 B:TRP122 4.6 6.2 1.0
CB B:TRP158 4.6 2.0 1.0
CZ2 B:TRP122 4.7 7.4 1.0
CG B:TRP158 4.8 5.0 1.0

Reference:

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
Page generated: Sat Aug 3 08:12:39 2024

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