Iron in PDB 2uyu: L-Rhamnulose-1-Phosphate Aldolase From Escherichia Coli (Mutant A88F- E192A)

All present enzymatic activity of L-Rhamnulose-1-Phosphate Aldolase From Escherichia Coli (Mutant A88F- E192A):
4.1.2.19;

The structure of L-Rhamnulose-1-Phosphate Aldolase From Escherichia Coli (Mutant A88F- E192A), PDB code: 2uyu was solved by D.Grueninger, G.E.Schulz, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	19.96 / 1.96
Space group	P 4 2 2
Cell size a, b, c (Å), α, β, γ (°)	87.097, 87.097, 170.340, 90.00, 90.00, 90.00
R / Rfree (%)	20.1 / 24.5

The structure of L-Rhamnulose-1-Phosphate Aldolase From Escherichia Coli (Mutant A88F- E192A) also contains other interesting chemical elements:

Zinc

(Zn)

2 atoms

The binding sites of Iron atom in the L-Rhamnulose-1-Phosphate Aldolase From Escherichia Coli (Mutant A88F- E192A) (pdb code 2uyu). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the L-Rhamnulose-1-Phosphate Aldolase From Escherichia Coli (Mutant A88F- E192A), PDB code: 2uyu:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the L-Rhamnulose-1-Phosphate Aldolase From Escherichia Coli (Mutant A88F- E192A)


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of L-Rhamnulose-1-Phosphate Aldolase From Escherichia Coli (Mutant A88F- E192A) within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe1276 b:25.9 occ:1.00 O A:HOH2125 1.8 28.8 1.0 O E:HOH2161 1.9 20.4 1.0 NE2 A:HIS204 2.0 31.5 1.0 O A:HOH2126 2.1 27.1 1.0 O A:HOH2123 2.1 30.5 1.0 OE1 E:GLU254 2.1 31.0 1.0 CE1 A:HIS204 2.9 28.7 1.0 CD2 A:HIS204 3.0 28.7 1.0 CD E:GLU254 3.2 30.7 1.0 OE2 E:GLU254 3.6 23.9 1.0 OE2 A:GLU200 3.8 35.6 1.0 CG2 A:THR158 4.0 29.1 1.0 ND1 A:HIS204 4.1 29.6 1.0 O E:HOH2160 4.1 31.1 1.0 CG A:HIS204 4.2 28.0 1.0 OG1 A:THR158 4.2 35.9 1.0 OE1 A:GLU200 4.3 33.6 1.0 O E:HOH2162 4.3 34.9 1.0 O A:HOH2114 4.3 37.2 1.0 CD A:GLU200 4.4 34.9 1.0 CG E:GLU254 4.5 27.8 1.0 CB A:THR158 4.5 31.2 1.0 CA A:GLY181 4.6 27.9 1.0 O A:HOH2107 4.6 38.1 1.0 CB E:GLU254 4.8 30.1 1.0 CB A:LYS203 5.0 29.9 1.0

Iron binding site 2 out of 2 in the L-Rhamnulose-1-Phosphate Aldolase From Escherichia Coli (Mutant A88F- E192A)


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of L-Rhamnulose-1-Phosphate Aldolase From Escherichia Coli (Mutant A88F- E192A) within 5.0Å range: probe atom residue distance (Å) B Occ E:Fe1276 b:56.8 occ:1.00 O E:HOH2123 2.3 37.8 1.0 O E:HOH2122 2.3 37.1 1.0 NE2 E:HIS204 2.4 31.1 1.0 O E:HOH2124 2.9 38.3 1.0 CE1 E:HIS204 3.3 28.6 1.0 CD2 E:HIS204 3.4 29.0 1.0 OE2 E:GLU200 4.1 35.9 1.0 CG2 E:THR158 4.2 28.8 1.0 OE1 E:GLU200 4.4 34.7 1.0 ND1 E:HIS204 4.4 30.1 1.0 CG E:HIS204 4.5 28.4 1.0 OG1 E:THR158 4.5 35.4 1.0 CB E:LYS203 4.6 29.9 1.0 CD E:GLU200 4.7 34.7 1.0 CB E:THR158 4.8 31.4 1.0 O E:HOH2120 5.0 59.9 1.0

D.Grueninger, N.Treiber, M.O.P.Ziegler, J.W.A.Koetter, M.-S.Schulze, G.E.Schulz. Designed Protein-Protein Association. Science V. 319 206 2008.
ISSN: ISSN 0036-8075
PubMed: 18187656
DOI: 10.1126/SCIENCE.1150421