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Atomistry » Iron » PDB 2rfc-2v1i » 2uyu | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Iron » PDB 2rfc-2v1i » 2uyu » |
Iron in PDB 2uyu: L-Rhamnulose-1-Phosphate Aldolase From Escherichia Coli (Mutant A88F- E192A)Enzymatic activity of 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; Protein crystallography data
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:
Other elements in 2uyu:
The structure of L-Rhamnulose-1-Phosphate Aldolase From Escherichia Coli (Mutant A88F- E192A) also contains other interesting chemical elements:
Iron Binding Sites:
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 2uyuGo back to![]() ![]()
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
Iron binding site 2 out of 2 in 2uyuGo back to![]() ![]()
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
Reference:
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.
Page generated: Thu Jul 17 04:05:44 2025
ISSN: ISSN 0036-8075 PubMed: 18187656 DOI: 10.1126/SCIENCE.1150421 |
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