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Iron in PDB 2r2f: Ribonucleotide Reductase R2F Protein From Salmonella Typhimurium (Oxidized)

Enzymatic activity of Ribonucleotide Reductase R2F Protein From Salmonella Typhimurium (Oxidized)

All present enzymatic activity of Ribonucleotide Reductase R2F Protein From Salmonella Typhimurium (Oxidized):
1.17.4.1;

Protein crystallography data

The structure of Ribonucleotide Reductase R2F Protein From Salmonella Typhimurium (Oxidized), PDB code: 2r2f was solved by H.Eklund, M.Eriksson, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 20.00 / 2.25
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 58.490, 71.740, 96.070, 90.00, 95.01, 90.00
R / Rfree (%) 22.8 / 26.8

Iron Binding Sites:

The binding sites of Iron atom in the Ribonucleotide Reductase R2F Protein From Salmonella Typhimurium (Oxidized) (pdb code 2r2f). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 4 binding sites of Iron where determined in the Ribonucleotide Reductase R2F Protein From Salmonella Typhimurium (Oxidized), PDB code: 2r2f:
Jump to Iron binding site number: 1; 2; 3; 4;

Iron binding site 1 out of 4 in 2r2f

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Iron binding site 1 out of 4 in the Ribonucleotide Reductase R2F Protein From Salmonella Typhimurium (Oxidized)


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Ribonucleotide Reductase R2F Protein From Salmonella Typhimurium (Oxidized) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe320

b:36.6
occ:0.89
FE1 A:FEO320 0.0 36.6 0.9
O A:FEO320 2.0 32.3 1.0
O A:HOH387 2.2 35.1 1.0
OE1 A:GLU98 2.2 25.5 1.0
ND1 A:HIS101 2.2 20.8 1.0
OD1 A:ASP67 2.3 34.2 1.0
O A:HOH386 2.6 28.2 1.0
OE1 A:GLU192 2.9 38.6 1.0
CE1 A:HIS101 3.1 21.2 1.0
CD A:GLU98 3.2 23.7 1.0
CG A:ASP67 3.3 32.7 1.0
CG A:HIS101 3.4 21.2 1.0
FE2 A:FEO320 3.4 32.3 1.0
OE2 A:GLU98 3.5 25.4 1.0
OD2 A:ASP67 3.6 36.0 1.0
CD A:GLU192 3.7 36.9 1.0
CB A:HIS101 3.8 20.9 1.0
OE2 A:GLU192 4.0 37.4 1.0
NE2 A:HIS101 4.2 21.2 1.0
CG2 A:ILE188 4.3 26.2 1.0
CD2 A:HIS101 4.4 21.4 1.0
CZ A:PHE162 4.5 40.5 1.0
CB A:ASP67 4.6 29.8 1.0
CE1 A:PHE162 4.6 40.9 1.0
CA A:GLU98 4.6 20.9 1.0
CG A:GLU98 4.6 22.4 1.0
ND1 A:HIS195 4.8 23.1 1.0
CE2 A:PHE162 4.8 40.9 1.0
CB A:GLU98 4.9 21.3 1.0
CD1 A:PHE162 4.9 40.9 1.0
CE1 A:HIS195 4.9 23.0 1.0
CG A:GLU192 5.0 34.3 1.0

Iron binding site 2 out of 4 in 2r2f

Go back to Iron Binding Sites List in 2r2f
Iron binding site 2 out of 4 in the Ribonucleotide Reductase R2F Protein From Salmonella Typhimurium (Oxidized)


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Ribonucleotide Reductase R2F Protein From Salmonella Typhimurium (Oxidized) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe320

b:32.3
occ:1.00
FE2 A:FEO320 0.0 32.3 1.0
O A:FEO320 1.7 32.3 1.0
OE2 A:GLU98 1.9 25.4 1.0
OE2 A:GLU192 2.1 37.4 1.0
OE2 A:GLU158 2.1 32.3 1.0
ND1 A:HIS195 2.3 23.1 1.0
O A:HOH386 2.5 28.2 1.0
CD A:GLU158 2.8 32.2 1.0
CD A:GLU98 3.0 23.7 1.0
CD A:GLU192 3.0 36.9 1.0
CE1 A:HIS195 3.3 23.0 1.0
OE1 A:GLU98 3.3 25.5 1.0
CG A:HIS195 3.3 22.9 1.0
CG A:GLU158 3.4 31.3 1.0
OE1 A:GLU192 3.4 38.6 1.0
FE1 A:FEO320 3.4 36.6 0.9
CB A:HIS195 3.6 22.1 1.0
OE1 A:GLU158 3.7 35.2 1.0
O A:HOH446 3.9 41.6 1.0
CG A:GLU98 4.3 22.4 1.0
CG A:GLU192 4.3 34.3 1.0
CB A:GLU158 4.3 28.3 1.0
CA A:GLU192 4.4 27.4 1.0
NE2 A:HIS195 4.4 22.6 1.0
CD2 A:HIS195 4.5 22.6 1.0
CG A:GLN70 4.5 31.8 1.0
CB A:GLU192 4.8 30.4 1.0
OD1 A:ASP67 4.8 34.2 1.0
CG2 A:ILE94 4.8 18.8 1.0
CE1 A:HIS101 4.9 21.2 1.0
O A:HOH387 4.9 35.1 1.0
ND1 A:HIS101 4.9 20.8 1.0
N A:GLU192 5.0 26.5 1.0

Iron binding site 3 out of 4 in 2r2f

Go back to Iron Binding Sites List in 2r2f
Iron binding site 3 out of 4 in the Ribonucleotide Reductase R2F Protein From Salmonella Typhimurium (Oxidized)


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 3 of Ribonucleotide Reductase R2F Protein From Salmonella Typhimurium (Oxidized) within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe320

b:47.3
occ:0.77
FE1 B:FEO320 0.0 47.3 0.8
O B:FEO320 1.9 41.5 1.0
OD1 B:ASP67 2.1 54.8 1.0
OE1 B:GLU98 2.3 37.9 1.0
ND1 B:HIS101 2.4 31.7 1.0
O B:HOH352 2.9 40.9 1.0
OE1 B:GLU192 3.0 45.6 1.0
CG B:ASP67 3.3 54.6 1.0
CE1 B:HIS101 3.4 31.7 1.0
CD B:GLU98 3.4 36.4 1.0
CG B:HIS101 3.4 31.6 1.0
FE2 B:FEO320 3.4 42.7 0.9
CB B:HIS101 3.7 31.7 1.0
OD2 B:ASP67 3.8 55.3 1.0
OE2 B:GLU98 3.8 37.2 1.0
CD B:GLU192 3.9 44.0 1.0
CE2 B:PHE162 3.9 61.6 1.0
OE2 B:GLU192 4.0 45.5 1.0
CZ B:PHE162 4.1 61.8 1.0
CB B:ASP67 4.4 54.1 1.0
CD2 B:PHE162 4.5 61.9 1.0
NE2 B:HIS101 4.5 31.9 1.0
CD2 B:HIS101 4.5 31.4 1.0
CG2 B:ILE188 4.6 38.3 1.0
CA B:GLU98 4.6 30.0 1.0
CG B:GLU98 4.7 33.9 1.0
CE1 B:PHE162 4.8 61.8 1.0
CB B:GLU98 4.9 31.0 1.0
CA B:ASP67 4.9 53.6 1.0

Iron binding site 4 out of 4 in 2r2f

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Iron binding site 4 out of 4 in the Ribonucleotide Reductase R2F Protein From Salmonella Typhimurium (Oxidized)


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 4 of Ribonucleotide Reductase R2F Protein From Salmonella Typhimurium (Oxidized) within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe320

b:42.7
occ:0.91
FE2 B:FEO320 0.0 42.7 0.9
O B:FEO320 1.9 41.5 1.0
OE2 B:GLU98 2.1 37.2 1.0
OE2 B:GLU192 2.2 45.5 1.0
ND1 B:HIS195 2.5 27.3 1.0
O B:HOH352 2.6 40.9 1.0
OE2 B:GLU158 2.7 48.9 1.0
CD B:GLU98 3.0 36.4 1.0
CD B:GLU192 3.1 44.0 1.0
CD B:GLU158 3.1 48.6 1.0
OE1 B:GLU98 3.2 37.9 1.0
CG B:GLU158 3.4 48.3 1.0
CE1 B:HIS195 3.4 26.9 1.0
FE1 B:FEO320 3.4 47.3 0.8
OE1 B:GLU192 3.5 45.6 1.0
CG B:HIS195 3.6 27.6 1.0
CB B:HIS195 3.9 28.9 1.0
OE1 B:GLU158 3.9 49.1 1.0
CG B:GLU192 4.4 41.6 1.0
CG B:GLU98 4.4 33.9 1.0
CB B:GLU158 4.4 47.2 1.0
CG B:GLN70 4.5 51.7 1.0
CA B:GLU192 4.5 35.0 1.0
NE2 B:HIS195 4.6 26.4 1.0
ND1 B:HIS101 4.6 31.7 1.0
CE1 B:HIS101 4.7 31.7 1.0
CD2 B:HIS195 4.7 27.4 1.0
CB B:GLU192 4.9 37.5 1.0
OD1 B:ASP67 5.0 54.8 1.0

Reference:

M.Eriksson, A.Jordan, H.Eklund. Structure of Salmonella Typhimurium Nrdf Ribonucleotide Reductase in Its Oxidized and Reduced Forms. Biochemistry V. 37 13359 1998.
ISSN: ISSN 0006-2960
PubMed: 9748343
DOI: 10.1021/BI981380S
Page generated: Sun Aug 4 02:04:32 2024

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