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Iron in PDB 1wb7: Iron Superoxide Dismutase (Fe-Sod) From the Hyperthermophile Sulfolobus Solfataricus. Crystal Structure of the Y41F Mutant.

Enzymatic activity of Iron Superoxide Dismutase (Fe-Sod) From the Hyperthermophile Sulfolobus Solfataricus. Crystal Structure of the Y41F Mutant.

All present enzymatic activity of Iron Superoxide Dismutase (Fe-Sod) From the Hyperthermophile Sulfolobus Solfataricus. Crystal Structure of the Y41F Mutant.:
1.15.1.1;

Protein crystallography data

The structure of Iron Superoxide Dismutase (Fe-Sod) From the Hyperthermophile Sulfolobus Solfataricus. Crystal Structure of the Y41F Mutant., PDB code: 1wb7 was solved by M.A.Gogliettino, F.Tanfani, A.Scire, T.Ursby, B.S.Adinolfi, T.Cacciamani, E.De Vendittis, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 29.07 / 2.24
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 75.188, 121.753, 59.420, 90.00, 128.74, 90.00
R / Rfree (%) 18.1 / 20.9

Iron Binding Sites:

The binding sites of Iron atom in the Iron Superoxide Dismutase (Fe-Sod) From the Hyperthermophile Sulfolobus Solfataricus. Crystal Structure of the Y41F Mutant. (pdb code 1wb7). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the Iron Superoxide Dismutase (Fe-Sod) From the Hyperthermophile Sulfolobus Solfataricus. Crystal Structure of the Y41F Mutant., PDB code: 1wb7:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in 1wb7

Go back to Iron Binding Sites List in 1wb7
Iron binding site 1 out of 2 in the Iron Superoxide Dismutase (Fe-Sod) From the Hyperthermophile Sulfolobus Solfataricus. Crystal Structure of the Y41F Mutant.


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Iron Superoxide Dismutase (Fe-Sod) From the Hyperthermophile Sulfolobus Solfataricus. Crystal Structure of the Y41F Mutant. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe212

b:14.6
occ:1.00
OD2 A:ASP170 1.9 13.8 1.0
NE2 A:HIS84 2.1 11.1 1.0
NE2 A:HIS174 2.1 16.2 1.0
NE2 A:HIS33 2.2 10.3 1.0
O A:HOH2088 2.4 29.1 1.0
CD2 A:HIS84 3.0 11.6 1.0
CG A:ASP170 3.1 14.0 1.0
CD2 A:HIS174 3.1 16.3 1.0
CE1 A:HIS84 3.1 11.9 1.0
CE1 A:HIS33 3.1 8.7 1.0
CD2 A:HIS33 3.2 8.3 1.0
CE1 A:HIS174 3.2 14.5 1.0
OD1 A:ASP170 3.5 16.1 1.0
ND1 A:HIS84 4.1 11.8 1.0
CG A:HIS84 4.2 10.4 1.0
ND1 A:HIS33 4.2 8.7 1.0
CG A:HIS174 4.2 16.1 1.0
ND1 A:HIS174 4.2 16.6 1.0
CG A:HIS33 4.3 9.7 1.0
CB A:ASP170 4.3 12.8 1.0
CH2 A:TRP135 4.4 10.8 1.0
CZ2 A:TRP135 4.5 8.6 1.0
CB A:PHE172 4.5 14.3 1.0
CB A:ALA175 4.8 15.0 1.0

Iron binding site 2 out of 2 in 1wb7

Go back to Iron Binding Sites List in 1wb7
Iron binding site 2 out of 2 in the Iron Superoxide Dismutase (Fe-Sod) From the Hyperthermophile Sulfolobus Solfataricus. Crystal Structure of the Y41F Mutant.


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Iron Superoxide Dismutase (Fe-Sod) From the Hyperthermophile Sulfolobus Solfataricus. Crystal Structure of the Y41F Mutant. within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe211

b:14.5
occ:1.00
OD2 B:ASP170 1.9 13.7 1.0
NE2 B:HIS174 2.1 16.2 1.0
NE2 B:HIS84 2.1 11.2 1.0
NE2 B:HIS33 2.2 10.3 1.0
O B:HOH2093 2.4 29.1 1.0
CG B:ASP170 3.0 14.0 1.0
CD2 B:HIS174 3.1 16.3 1.0
CD2 B:HIS84 3.1 11.6 1.0
CE1 B:HIS84 3.1 11.8 1.0
CE1 B:HIS33 3.1 8.7 1.0
CE1 B:HIS174 3.2 14.5 1.0
CD2 B:HIS33 3.2 8.3 1.0
OD1 B:ASP170 3.5 16.1 1.0
ND1 B:HIS84 4.2 11.8 1.0
CG B:HIS84 4.2 10.4 1.0
ND1 B:HIS33 4.2 8.7 1.0
CG B:HIS174 4.2 16.1 1.0
ND1 B:HIS174 4.2 16.6 1.0
CG B:HIS33 4.3 9.7 1.0
CB B:ASP170 4.3 12.8 1.0
CH2 B:TRP135 4.4 10.8 1.0
CZ2 B:TRP135 4.5 8.6 1.0
CB B:PHE172 4.5 14.2 1.0
CB B:ALA175 4.8 15.0 1.0

Reference:

M.A.Gogliettino, F.Tanfani, A.Scire, T.Ursby, B.S.Adinolfi, T.Cacciamani, E.De Vendittis. The Role of TYR41 and HIS155 in the Functional Properties of Superoxide Dismutase From the Archaeon Sulfolobus Solfataricus Biochemistry V. 43 2199 2004.
ISSN: ISSN 0006-2960
PubMed: 14979716
DOI: 10.1021/BI035661Y
Page generated: Sun Dec 13 14:35:05 2020

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