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Iron in PDB 1av8: Ribonucleotide Reductase R2 Subunit From E. Coli

Enzymatic activity of Ribonucleotide Reductase R2 Subunit From E. Coli

All present enzymatic activity of Ribonucleotide Reductase R2 Subunit From E. Coli:
1.17.4.1;

Protein crystallography data

The structure of Ribonucleotide Reductase R2 Subunit From E. Coli, PDB code: 1av8 was solved by S.Han, A.Arvai, J.A.Tainer, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 7.00 / 2.80
Space group P 61
Cell size a, b, c (Å), α, β, γ (°) 139.700, 139.700, 110.600, 90.00, 90.00, 120.00
R / Rfree (%) 13.9 / 19.2

Iron Binding Sites:

The binding sites of Iron atom in the Ribonucleotide Reductase R2 Subunit From E. Coli (pdb code 1av8). 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 R2 Subunit From E. Coli, PDB code: 1av8:
Jump to Iron binding site number: 1; 2; 3; 4;

Iron binding site 1 out of 4 in 1av8

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Iron binding site 1 out of 4 in the Ribonucleotide Reductase R2 Subunit From E. Coli


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Ribonucleotide Reductase R2 Subunit From E. Coli within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe401

b:25.5
occ:1.00
FE1 A:FEO401 0.0 25.5 1.0
OE1 A:GLU115 2.0 25.3 1.0
ND1 A:HIS118 2.0 21.4 1.0
O A:HOH1202 2.1 44.5 1.0
O A:FEO401 2.3 42.1 1.0
OD2 A:ASP84 2.5 26.6 1.0
OD1 A:ASP84 2.5 27.8 1.0
CG A:ASP84 2.8 28.9 1.0
CE1 A:HIS118 2.9 19.7 1.0
O A:HOH1201 3.0 41.1 1.0
CD A:GLU115 3.0 25.8 1.0
CG A:HIS118 3.2 22.4 1.0
FE2 A:FEO401 3.3 21.5 1.0
OE2 A:GLU115 3.5 29.3 1.0
CB A:HIS118 3.7 20.9 1.0
OE2 A:GLU238 3.9 23.1 1.0
NE2 A:HIS118 4.1 16.7 1.0
CB A:ASP84 4.2 24.3 1.0
CD2 A:HIS118 4.3 20.4 1.0
OE1 A:GLU238 4.3 26.6 1.0
CG A:GLU115 4.4 23.0 1.0
CE1 A:HIS241 4.4 15.7 1.0
CD A:GLU238 4.4 21.1 1.0
CG2 A:ILE234 4.4 11.0 1.0
CZ A:PHE208 4.4 33.2 1.0
CA A:GLU115 4.5 19.8 1.0
ND1 A:HIS241 4.6 16.5 1.0
CB A:GLU115 4.6 21.2 1.0
CE2 A:PHE208 4.7 34.5 1.0
CE1 A:PHE208 4.9 30.2 1.0

Iron binding site 2 out of 4 in 1av8

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Iron binding site 2 out of 4 in the Ribonucleotide Reductase R2 Subunit From E. Coli


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Ribonucleotide Reductase R2 Subunit From E. Coli within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe401

b:21.5
occ:1.00
FE2 A:FEO401 0.0 21.5 1.0
OE2 A:GLU204 2.0 18.2 1.0
OE1 A:GLU238 2.0 26.6 1.0
OE2 A:GLU115 2.0 29.3 1.0
ND1 A:HIS241 2.1 16.5 1.0
O A:FEO401 2.1 42.1 1.0
O A:HOH1201 2.2 41.1 1.0
CE1 A:HIS241 2.9 15.7 1.0
CD A:GLU115 2.9 25.8 1.0
CD A:GLU238 2.9 21.1 1.0
CD A:GLU204 3.1 23.9 1.0
OE1 A:GLU115 3.2 25.3 1.0
OE2 A:GLU238 3.2 23.1 1.0
CG A:HIS241 3.2 18.3 1.0
FE1 A:FEO401 3.3 25.5 1.0
CB A:HIS241 3.7 15.2 1.0
CG A:GLU204 3.7 23.0 1.0
OE1 A:GLU204 4.1 31.7 1.0
NE2 A:HIS241 4.1 13.9 1.0
NE1 A:TRP111 4.1 22.9 1.0
CD2 A:HIS241 4.2 15.0 1.0
CG A:GLU115 4.3 23.0 1.0
CG A:GLU238 4.3 15.9 1.0
O A:HOH1202 4.4 44.5 1.0
OD1 A:ASP84 4.4 27.8 1.0
NE2 A:GLN87 4.5 26.6 1.0
CB A:GLU204 4.5 18.5 1.0
CA A:GLU238 4.5 16.0 1.0
CE1 A:HIS118 4.6 19.7 1.0
ND1 A:HIS118 4.7 21.4 1.0
CD1 A:TRP111 4.7 19.6 1.0
CB A:GLU238 4.8 13.7 1.0
CG A:GLN87 4.9 26.5 1.0

Iron binding site 3 out of 4 in 1av8

Go back to Iron Binding Sites List in 1av8
Iron binding site 3 out of 4 in the Ribonucleotide Reductase R2 Subunit From E. Coli


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 3 of Ribonucleotide Reductase R2 Subunit From E. Coli within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe402

b:24.5
occ:1.00
FE1 B:FEO402 0.0 24.5 1.0
OE1 B:GLU115 2.0 26.4 1.0
ND1 B:HIS118 2.0 14.2 1.0
O B:FEO402 2.1 37.4 1.0
O B:HOH1204 2.3 44.3 1.0
OD2 B:ASP84 2.5 26.6 1.0
OD1 B:ASP84 2.5 20.4 1.0
CG B:ASP84 2.8 23.5 1.0
CE1 B:HIS118 2.8 15.7 1.0
CD B:GLU115 3.1 23.1 1.0
CG B:HIS118 3.1 16.6 1.0
O B:HOH1203 3.2 35.5 1.0
FE2 B:FEO402 3.5 20.8 1.0
OE2 B:GLU115 3.5 26.6 1.0
CB B:HIS118 3.7 15.8 1.0
OE2 B:GLU238 3.9 34.3 1.0
NE2 B:HIS118 4.0 15.2 1.0
CD2 B:HIS118 4.2 17.2 1.0
CB B:ASP84 4.2 22.1 1.0
OE1 B:GLU238 4.3 31.8 1.0
CG B:GLU115 4.3 21.9 1.0
CA B:GLU115 4.3 19.2 1.0
CG2 B:ILE234 4.4 13.9 1.0
CD B:GLU238 4.4 31.0 1.0
CE1 B:HIS241 4.5 20.3 1.0
ND1 B:HIS241 4.5 21.6 1.0
CZ B:PHE208 4.5 37.6 1.0
CB B:GLU115 4.6 18.0 1.0
CE2 B:PHE208 4.7 40.8 1.0
CE1 B:PHE208 5.0 37.5 1.0
O B:GLU115 5.0 23.8 1.0

Iron binding site 4 out of 4 in 1av8

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Iron binding site 4 out of 4 in the Ribonucleotide Reductase R2 Subunit From E. Coli


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 4 of Ribonucleotide Reductase R2 Subunit From E. Coli within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe402

b:20.8
occ:1.00
FE2 B:FEO402 0.0 20.8 1.0
OE1 B:GLU238 1.9 31.8 1.0
OE2 B:GLU204 1.9 25.9 1.0
O B:HOH1203 2.1 35.5 1.0
O B:FEO402 2.1 37.4 1.0
OE2 B:GLU115 2.1 26.6 1.0
ND1 B:HIS241 2.1 21.6 1.0
CD B:GLU238 2.9 31.0 1.0
CD B:GLU204 2.9 29.2 1.0
CD B:GLU115 3.0 23.1 1.0
CE1 B:HIS241 3.1 20.3 1.0
CG B:HIS241 3.2 23.8 1.0
OE2 B:GLU238 3.2 34.3 1.0
OE1 B:GLU115 3.3 26.4 1.0
FE1 B:FEO402 3.5 24.5 1.0
CB B:HIS241 3.5 23.0 1.0
CG B:GLU204 3.6 30.0 1.0
OE1 B:GLU204 3.8 36.2 1.0
NE1 B:TRP111 4.0 25.2 1.0
CG B:GLU238 4.2 26.7 1.0
O B:HOH1204 4.2 44.3 1.0
NE2 B:HIS241 4.2 22.3 1.0
CD2 B:HIS241 4.3 20.2 1.0
CG B:GLU115 4.4 21.9 1.0
CB B:GLU204 4.4 25.1 1.0
NE2 B:GLN87 4.4 28.9 1.0
CA B:GLU238 4.5 21.9 1.0
OD1 B:ASP84 4.5 20.4 1.0
CD1 B:TRP111 4.6 27.4 1.0
CB B:GLU238 4.8 20.3 1.0
CE1 B:HIS118 4.8 15.7 1.0
ND1 B:HIS118 4.8 14.2 1.0
CG B:GLN87 5.0 21.7 1.0

Reference:

W.Tong, D.Burdi, P.Riggs-Gelasco, S.Chen, D.Edmondson, B.H.Huynh, J.Stubbe, S.Han, A.Arvai, J.A.Tainer. Characterization of Y122F R2 of Escherichia Coli Ribonucleotide Reductase By Time-Resolved Physical Biochemical Methods and X-Ray Crystallography. Biochemistry V. 37 5840 1998.
ISSN: ISSN 0006-2960
PubMed: 9558317
DOI: 10.1021/BI9728811
Page generated: Sat Aug 3 02:21:08 2024

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