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Iron in PDB 1rib: Structure and Function of the Escherichia Coli Ribonucleotide Reductase Protein R2

Enzymatic activity of Structure and Function of the Escherichia Coli Ribonucleotide Reductase Protein R2

All present enzymatic activity of Structure and Function of the Escherichia Coli Ribonucleotide Reductase Protein R2:
1.17.4.1;

Protein crystallography data

The structure of Structure and Function of the Escherichia Coli Ribonucleotide Reductase Protein R2, PDB code: 1rib was solved by H.Eklund, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 7.00 / 2.20
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 74.300, 85.500, 115.700, 90.00, 90.00, 90.00
R / Rfree (%) 17.5 / n/a

Iron Binding Sites:

The binding sites of Iron atom in the Structure and Function of the Escherichia Coli Ribonucleotide Reductase Protein R2 (pdb code 1rib). 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 and Function of the Escherichia Coli Ribonucleotide Reductase Protein R2, PDB code: 1rib:
Jump to Iron binding site number: 1; 2; 3; 4;

Iron binding site 1 out of 4 in 1rib

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Iron binding site 1 out of 4 in the Structure and Function of the Escherichia Coli Ribonucleotide Reductase Protein R2


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Structure and Function of the Escherichia Coli Ribonucleotide Reductase Protein R2 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe401

b:21.5
occ:0.90
FE1 A:FEO401 0.0 21.5 0.9
OE1 A:GLU115 1.8 18.0 1.0
O A:HOH749 2.1 31.5 1.0
ND1 A:HIS118 2.1 7.3 1.0
OD2 A:ASP84 2.2 18.0 1.0
O A:FEO401 2.2 34.9 1.0
OD1 A:ASP84 2.5 18.9 1.0
CG A:ASP84 2.6 17.3 1.0
CD A:GLU115 2.9 15.7 1.0
CE1 A:HIS118 3.0 7.9 1.0
O A:HOH522 3.1 30.9 1.0
CG A:HIS118 3.2 9.0 1.0
OE2 A:GLU115 3.4 16.6 1.0
FE2 A:FEO401 3.4 12.9 1.0
CB A:HIS118 3.8 13.2 1.0
OE1 A:GLU238 4.0 23.4 1.0
CB A:ASP84 4.1 14.2 1.0
NE2 A:HIS118 4.2 9.0 1.0
CG A:GLU115 4.2 15.5 1.0
CD2 A:HIS118 4.3 9.9 1.0
OE2 A:GLU238 4.4 17.4 1.0
CA A:GLU115 4.4 13.7 1.0
CB A:GLU115 4.5 14.5 1.0
CD A:GLU238 4.5 20.9 1.0
CE2 A:PHE208 4.5 18.2 1.0
CZ A:PHE208 4.5 17.4 1.0
CG2 A:ILE234 4.6 11.3 1.0
ND1 A:HIS241 4.7 9.8 1.0
CE1 A:HIS241 4.7 9.3 1.0

Iron binding site 2 out of 4 in 1rib

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Iron binding site 2 out of 4 in the Structure and Function of the Escherichia Coli Ribonucleotide Reductase Protein R2


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Structure and Function of the Escherichia Coli Ribonucleotide Reductase Protein R2 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe401

b:12.9
occ:1.00
FE2 A:FEO401 0.0 12.9 1.0
OE2 A:GLU115 2.0 16.6 1.0
O A:FEO401 2.1 34.9 1.0
OE2 A:GLU238 2.1 17.4 1.0
OE2 A:GLU204 2.1 22.3 1.0
O A:HOH522 2.3 30.9 1.0
ND1 A:HIS241 2.3 9.8 1.0
CD A:GLU115 2.9 15.7 1.0
CD A:GLU238 3.1 20.9 1.0
OE1 A:GLU115 3.1 18.0 1.0
CD A:GLU204 3.2 22.4 1.0
CE1 A:HIS241 3.2 9.3 1.0
CG A:HIS241 3.3 11.8 1.0
FE1 A:FEO401 3.4 21.5 0.9
OE1 A:GLU238 3.6 23.4 1.0
CB A:HIS241 3.7 10.0 1.0
CG A:GLU204 3.9 20.5 1.0
NE1 A:TRP111 4.1 13.5 1.0
OE1 A:GLU204 4.1 25.6 1.0
O A:HOH749 4.2 31.5 1.0
CG A:GLU115 4.3 15.5 1.0
NE2 A:HIS241 4.4 12.4 1.0
OD1 A:ASP84 4.4 18.9 1.0
CG A:GLU238 4.4 16.7 1.0
CD1 A:TRP111 4.4 13.3 1.0
CD2 A:HIS241 4.4 10.8 1.0
CA A:GLU238 4.6 15.0 1.0
CB A:GLU204 4.7 17.7 1.0
CE1 A:HIS118 4.9 7.9 1.0
CB A:GLU238 4.9 13.5 1.0
ND1 A:HIS118 4.9 7.3 1.0

Iron binding site 3 out of 4 in 1rib

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Iron binding site 3 out of 4 in the Structure and Function of the Escherichia Coli Ribonucleotide Reductase Protein R2


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 3 of Structure and Function of the Escherichia Coli Ribonucleotide Reductase Protein R2 within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe402

b:22.9
occ:0.90
FE1 B:FEO402 0.0 22.9 0.9
O B:FEO402 1.8 24.8 1.0
ND1 B:HIS118 2.0 9.6 1.0
OE1 B:GLU115 2.0 14.6 1.0
O B:HOH712 2.1 31.4 1.0
OD2 B:ASP84 2.5 20.8 1.0
OD1 B:ASP84 2.6 22.0 1.0
CE1 B:HIS118 2.7 10.9 1.0
CG B:ASP84 2.8 20.0 1.0
O B:HOH640 3.1 24.9 1.0
CG B:HIS118 3.1 10.6 1.0
CD B:GLU115 3.1 13.9 1.0
FE2 B:FEO402 3.3 20.0 1.0
OE2 B:GLU115 3.6 17.3 1.0
OE2 B:GLU238 3.8 25.9 1.0
CB B:HIS118 3.8 12.4 1.0
NE2 B:HIS118 3.9 10.4 1.0
CD2 B:HIS118 4.2 9.6 1.0
CB B:ASP84 4.2 17.9 1.0
CG B:GLU115 4.4 11.7 1.0
CA B:GLU115 4.4 11.7 1.0
CD B:GLU238 4.5 22.3 1.0
CG2 B:ILE234 4.5 8.1 1.0
OE1 B:GLU238 4.5 22.3 1.0
CZ B:PHE208 4.5 19.8 1.0
CB B:GLU115 4.6 10.8 1.0
CE1 B:HIS241 4.6 8.3 1.0
CE2 B:PHE208 4.6 23.1 1.0
ND1 B:HIS241 4.6 9.5 1.0

Iron binding site 4 out of 4 in 1rib

Go back to Iron Binding Sites List in 1rib
Iron binding site 4 out of 4 in the Structure and Function of the Escherichia Coli Ribonucleotide Reductase Protein R2


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 4 of Structure and Function of the Escherichia Coli Ribonucleotide Reductase Protein R2 within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe402

b:20.0
occ:1.00
FE2 B:FEO402 0.0 20.0 1.0
O B:FEO402 1.9 24.8 1.0
OE2 B:GLU204 2.0 15.6 1.0
OE1 B:GLU238 2.1 22.3 1.0
O B:HOH640 2.2 24.9 1.0
ND1 B:HIS241 2.4 9.5 1.0
OE2 B:GLU115 2.4 17.3 1.0
CD B:GLU238 2.9 22.3 1.0
CD B:GLU204 3.0 16.9 1.0
CD B:GLU115 3.1 13.9 1.0
OE2 B:GLU238 3.1 25.9 1.0
OE1 B:GLU115 3.2 14.6 1.0
CE1 B:HIS241 3.2 8.3 1.0
FE1 B:FEO402 3.3 22.9 0.9
CG B:HIS241 3.4 8.8 1.0
CG B:GLU204 3.6 19.0 1.0
CB B:HIS241 3.8 11.2 1.0
OE1 B:GLU204 4.0 16.3 1.0
NE1 B:TRP111 4.2 11.4 1.0
O B:HOH712 4.2 31.4 1.0
CG B:GLU238 4.3 19.7 1.0
NE2 B:HIS241 4.4 8.0 1.0
CB B:GLU204 4.5 19.2 1.0
OD1 B:ASP84 4.5 22.0 1.0
CD2 B:HIS241 4.5 9.1 1.0
CG B:GLU115 4.5 11.7 1.0
CA B:GLU238 4.6 14.8 1.0
CE1 B:HIS118 4.7 10.9 1.0
CD1 B:TRP111 4.7 10.7 1.0
ND1 B:HIS118 4.7 9.6 1.0
NE2 B:GLN87 4.7 17.4 1.0
CB B:GLU238 5.0 16.8 1.0

Reference:

P.Nordlund, H.Eklund. Structure and Function of the Escherichia Coli Ribonucleotide Reductase Protein R2. J.Mol.Biol. V. 232 123 1993.
ISSN: ISSN 0022-2836
PubMed: 8331655
DOI: 10.1006/JMBI.1993.1374
Page generated: Sat Aug 3 14:15:52 2024

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