Atomistry » Iron » PDB 1yev-1yqo » 1yfd
Atomistry »
  Iron »
    PDB 1yev-1yqo »
      1yfd »

Iron in PDB 1yfd: Crystal Structure of the Y122H Mutant of Ribonucleotide Reductase R2 Protein From E. Coli

Enzymatic activity of Crystal Structure of the Y122H Mutant of Ribonucleotide Reductase R2 Protein From E. Coli

All present enzymatic activity of Crystal Structure of the Y122H Mutant of Ribonucleotide Reductase R2 Protein From E. Coli:
1.17.4.1;

Protein crystallography data

The structure of Crystal Structure of the Y122H Mutant of Ribonucleotide Reductase R2 Protein From E. Coli, PDB code: 1yfd was solved by M.Kolberg, D.T.Logan, G.Bleifuss, S.Poetsch, B.M.Sjoeberg, A.Graeslund, W.Lubitz, G.Lassmann, F.Lendzian, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 19.46 / 1.90
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 74.040, 84.740, 115.030, 90.00, 90.00, 90.00
R / Rfree (%) 17.3 / 20.6

Other elements in 1yfd:

The structure of Crystal Structure of the Y122H Mutant of Ribonucleotide Reductase R2 Protein From E. Coli also contains other interesting chemical elements:

Mercury (Hg) 13 atoms

Iron Binding Sites:

The binding sites of Iron atom in the Crystal Structure of the Y122H Mutant of Ribonucleotide Reductase R2 Protein From E. Coli (pdb code 1yfd). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 4 binding sites of Iron where determined in the Crystal Structure of the Y122H Mutant of Ribonucleotide Reductase R2 Protein From E. Coli, PDB code: 1yfd:
Jump to Iron binding site number: 1; 2; 3; 4;

Iron binding site 1 out of 4 in 1yfd

Go back to Iron Binding Sites List in 1yfd
Iron binding site 1 out of 4 in the Crystal Structure of the Y122H Mutant of Ribonucleotide Reductase R2 Protein 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 Crystal Structure of the Y122H Mutant of Ribonucleotide Reductase R2 Protein From E. Coli within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe501

b:12.7
occ:1.00
FE1 A:FEO501 0.0 12.7 1.0
O A:FEO501 1.8 13.3 1.0
OD1 A:ASP84 2.0 13.9 1.0
OE1 A:GLU115 2.1 15.3 1.0
ND1 A:HIS118 2.1 7.6 1.0
O A:HOH610 2.2 12.8 1.0
O A:HOH612 2.7 32.9 1.0
CE1 A:HIS118 3.0 10.0 1.0
CD A:GLU115 3.1 13.4 1.0
CG A:ASP84 3.1 14.4 1.0
CG A:HIS118 3.2 8.2 1.0
O A:HOH611 3.5 15.0 1.0
FE2 A:FEO501 3.5 12.4 1.0
OE2 A:GLU115 3.6 10.9 1.0
OD2 A:ASP84 3.6 16.4 1.0
CB A:HIS118 3.6 8.8 1.0
OE2 A:GLU238 3.9 24.6 1.0
NE2 A:HIS118 4.1 9.6 1.0
CD2 A:HIS118 4.3 7.7 1.0
CB A:ASP84 4.4 12.0 1.0
CG A:GLU115 4.4 10.9 1.0
CE2 A:PHE208 4.4 21.9 1.0
CG2 A:ILE234 4.4 12.7 1.0
CA A:GLU115 4.5 8.4 1.0
OE1 A:GLU238 4.5 17.1 1.0
CD A:GLU238 4.5 19.9 1.0
CZ A:PHE208 4.6 22.2 1.0
CB A:GLU115 4.6 9.4 1.0
CE1 A:HIS241 4.7 7.5 1.0
ND1 A:HIS241 4.8 8.2 1.0
CA A:ASP84 4.9 11.9 1.0
CD2 A:PHE208 5.0 23.6 1.0

Iron binding site 2 out of 4 in 1yfd

Go back to Iron Binding Sites List in 1yfd
Iron binding site 2 out of 4 in the Crystal Structure of the Y122H Mutant of Ribonucleotide Reductase R2 Protein 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 Crystal Structure of the Y122H Mutant of Ribonucleotide Reductase R2 Protein From E. Coli within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe501

b:12.4
occ:1.00
FE2 A:FEO501 0.0 12.4 1.0
OE1 A:GLU238 2.0 17.1 1.0
OE2 A:GLU115 2.0 10.9 1.0
OE1 A:GLU204 2.1 16.2 1.0
O A:FEO501 2.2 13.3 1.0
O A:HOH611 2.2 15.0 1.0
ND1 A:HIS241 2.3 8.2 1.0
CD A:GLU115 3.0 13.4 1.0
CD A:GLU238 3.0 19.9 1.0
CD A:GLU204 3.1 14.4 1.0
CE1 A:HIS241 3.2 7.5 1.0
OE1 A:GLU115 3.3 15.3 1.0
OE2 A:GLU238 3.4 24.6 1.0
CG A:HIS241 3.4 6.8 1.0
FE1 A:FEO501 3.5 12.7 1.0
O A:HOH612 3.7 32.9 1.0
CB A:HIS241 3.8 7.8 1.0
CG A:GLU204 3.8 15.3 1.0
NE1 A:TRP111 4.0 8.4 1.0
OE2 A:GLU204 4.1 16.4 1.0
CG A:GLU238 4.3 14.3 1.0
CG A:GLU115 4.4 10.9 1.0
NE2 A:HIS241 4.4 6.6 1.0
CB A:GLU204 4.5 13.6 1.0
O A:HOH610 4.5 12.8 1.0
CD2 A:HIS241 4.5 7.3 1.0
CA A:GLU238 4.6 11.4 1.0
CD1 A:TRP111 4.6 8.2 1.0
CE1 A:HIS118 4.7 10.0 1.0
CB A:GLU238 4.8 12.4 1.0
ND1 A:HIS118 4.8 7.6 1.0
OE1 A:GLN87 4.9 15.1 1.0

Iron binding site 3 out of 4 in 1yfd

Go back to Iron Binding Sites List in 1yfd
Iron binding site 3 out of 4 in the Crystal Structure of the Y122H Mutant of Ribonucleotide Reductase R2 Protein 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 Crystal Structure of the Y122H Mutant of Ribonucleotide Reductase R2 Protein From E. Coli within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe502

b:12.6
occ:1.00
FE1 B:FEO502 0.0 12.6 1.0
OD1 B:ASP84 2.0 11.9 1.0
OE1 B:GLU115 2.1 10.7 1.0
O B:FEO502 2.1 10.1 1.0
O B:HOH614 2.1 26.3 1.0
ND1 B:HIS118 2.2 7.7 1.0
O B:HOH616 2.5 26.7 1.0
CE1 B:HIS118 3.0 9.2 1.0
CG B:ASP84 3.1 13.5 1.0
CD B:GLU115 3.2 7.6 1.0
CG B:HIS118 3.3 7.8 1.0
O B:HOH615 3.3 20.7 1.0
FE2 B:FEO502 3.4 11.4 1.0
OD2 B:ASP84 3.5 15.9 1.0
OE2 B:GLU115 3.6 9.7 1.0
OE1 B:GLU238 3.8 22.7 1.0
CB B:HIS118 3.8 8.0 1.0
NE2 B:HIS118 4.2 8.1 1.0
CD2 B:HIS118 4.4 9.2 1.0
CB B:ASP84 4.4 10.8 1.0
CE2 B:PHE208 4.4 20.3 1.0
CG B:GLU115 4.4 6.8 1.0
OE2 B:GLU238 4.5 14.5 1.0
CG2 B:ILE234 4.5 9.6 1.0
CD B:GLU238 4.5 17.4 1.0
CA B:GLU115 4.5 7.5 1.0
CE1 B:HIS241 4.6 8.7 1.0
CB B:GLU115 4.7 7.6 1.0
CZ B:PHE208 4.7 20.3 1.0
ND1 B:HIS241 4.8 7.4 1.0
CA B:ASP84 4.8 10.1 1.0
CD2 B:PHE208 4.9 21.3 1.0

Iron binding site 4 out of 4 in 1yfd

Go back to Iron Binding Sites List in 1yfd
Iron binding site 4 out of 4 in the Crystal Structure of the Y122H Mutant of Ribonucleotide Reductase R2 Protein 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 Crystal Structure of the Y122H Mutant of Ribonucleotide Reductase R2 Protein From E. Coli within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe502

b:11.4
occ:1.00
FE2 B:FEO502 0.0 11.4 1.0
O B:FEO502 1.9 10.1 1.0
OE1 B:GLU204 1.9 13.3 1.0
OE2 B:GLU238 2.1 14.5 1.0
OE2 B:GLU115 2.1 9.7 1.0
ND1 B:HIS241 2.2 7.4 1.0
O B:HOH615 2.4 20.7 1.0
CD B:GLU115 3.0 7.6 1.0
CD B:GLU238 3.0 17.4 1.0
CD B:GLU204 3.1 16.2 1.0
CE1 B:HIS241 3.1 8.7 1.0
OE1 B:GLU115 3.3 10.7 1.0
CG B:HIS241 3.4 7.8 1.0
OE1 B:GLU238 3.4 22.7 1.0
FE1 B:FEO502 3.4 12.6 1.0
CG B:GLU204 3.8 16.4 1.0
CB B:HIS241 3.8 9.1 1.0
O B:HOH616 3.8 26.7 1.0
OE2 B:GLU204 4.1 19.7 1.0
NE1 B:TRP111 4.1 6.3 1.0
NE2 B:HIS241 4.2 6.6 1.0
O B:HOH614 4.3 26.3 1.0
CG B:GLU238 4.4 14.6 1.0
CG B:GLU115 4.4 6.8 1.0
CD2 B:HIS241 4.4 8.2 1.0
CB B:GLU204 4.4 14.6 1.0
CA B:GLU238 4.6 11.0 1.0
CD1 B:TRP111 4.6 5.7 1.0
CE1 B:HIS118 4.7 9.2 1.0
ND1 B:HIS118 4.8 7.7 1.0
OE1 B:GLN87 4.9 16.9 1.0
CB B:GLU238 4.9 11.7 1.0

Reference:

M.Kolberg, D.T.Logan, G.Bleifuss, S.Poetsch, B.M.Sjoeberg, A.Graeslund, W.Lubitz, G.Lassmann, F.Lendzian. A New Tyrosyl Radical on PHE208 As Ligand to the Diiron Center in Escherichia Coli Ribonucleotide Reductase, Mutant R2-Y122H. Combined X-Ray Diffraction and Epr/Endor Studies J.Biol.Chem. V. 280 11233 2005.
ISSN: ISSN 0021-9258
PubMed: 15634667
DOI: 10.1074/JBC.M414634200
Page generated: Sat Aug 3 17:44:08 2024

Last articles

Zn in 9JPJ
Zn in 9JP7
Zn in 9JPK
Zn in 9JPL
Zn in 9GN6
Zn in 9GN7
Zn in 9GKU
Zn in 9GKW
Zn in 9GKX
Zn in 9GL0
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy