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Iron in PDB 1ra5: Bacterial Cytosine Deaminase D314A Mutant Bound to 5-Fluoro-4-(S)- Hydroxyl-3,4-Dihydropyrimidine.

Enzymatic activity of Bacterial Cytosine Deaminase D314A Mutant Bound to 5-Fluoro-4-(S)- Hydroxyl-3,4-Dihydropyrimidine.

All present enzymatic activity of Bacterial Cytosine Deaminase D314A Mutant Bound to 5-Fluoro-4-(S)- Hydroxyl-3,4-Dihydropyrimidine.:
3.5.4.1;

Protein crystallography data

The structure of Bacterial Cytosine Deaminase D314A Mutant Bound to 5-Fluoro-4-(S)- Hydroxyl-3,4-Dihydropyrimidine., PDB code: 1ra5 was solved by S.D.Mahan, G.C.Ireton, B.L.Stoddard, M.E.Black, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 19.97 / 1.40
Space group H 3 2
Cell size a, b, c (Å), α, β, γ (°) 109.336, 109.336, 240.639, 90.00, 90.00, 120.00
R / Rfree (%) 18.3 / 19.3

Other elements in 1ra5:

The structure of Bacterial Cytosine Deaminase D314A Mutant Bound to 5-Fluoro-4-(S)- Hydroxyl-3,4-Dihydropyrimidine. also contains other interesting chemical elements:

Fluorine (F) 1 atom

Iron Binding Sites:

The binding sites of Iron atom in the Bacterial Cytosine Deaminase D314A Mutant Bound to 5-Fluoro-4-(S)- Hydroxyl-3,4-Dihydropyrimidine. (pdb code 1ra5). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total only one binding site of Iron was determined in the Bacterial Cytosine Deaminase D314A Mutant Bound to 5-Fluoro-4-(S)- Hydroxyl-3,4-Dihydropyrimidine., PDB code: 1ra5:

Iron binding site 1 out of 1 in 1ra5

Go back to Iron Binding Sites List in 1ra5
Iron binding site 1 out of 1 in the Bacterial Cytosine Deaminase D314A Mutant Bound to 5-Fluoro-4-(S)- Hydroxyl-3,4-Dihydropyrimidine.


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Bacterial Cytosine Deaminase D314A Mutant Bound to 5-Fluoro-4-(S)- Hydroxyl-3,4-Dihydropyrimidine. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe500

b:14.4
occ:1.00
 O4 A:FPY501 2.0 15.6 1.0
NE2 A:HIS61 2.0 10.2 1.0
NE2 A:HIS63 2.1 11.4 1.0
NE2 A:HIS214 2.3 14.1 1.0
OD2 A:ASP313 2.5 15.6 1.0
CE1 A:HIS61 3.0 10.7 1.0
CD2 A:HIS63 3.0 12.3 1.0
CE1 A:HIS63 3.1 13.5 1.0
CD2 A:HIS61 3.1 10.6 1.0
CE1 A:HIS214 3.2 11.3 1.0
C4 A:FPY501 3.2 15.2 1.0
CD2 A:HIS214 3.3 12.4 1.0
C5 A:FPY501 3.4 15.8 1.0
CG A:ASP313 3.4 14.6 1.0
OD1 A:ASP313 3.6 14.1 1.0
NE2 A:HIS246 3.7 11.8 1.0
N3 A:FPY501 3.7 13.9 1.0
F5 A:FPY501 3.8 15.8 1.0
C6 A:FPY501 3.9 15.4 1.0
ND1 A:HIS61 4.1 10.5 1.0
ND1 A:HIS63 4.2 12.5 1.0
CG A:HIS63 4.2 12.0 1.0
CG A:HIS61 4.2 9.2 1.0
C2 A:FPY501 4.2 15.2 1.0
N1 A:FPY501 4.2 15.9 1.0
ND1 A:HIS214 4.3 11.7 1.0
CG A:HIS214 4.4 10.5 1.0
CD2 A:HIS246 4.5 11.8 1.0
CE1 A:HIS246 4.6 12.4 1.0
CB A:ASP313 4.8 12.1 1.0
CD2 A:HIS122 4.8 10.8 1.0

Reference:

S.D.Mahan, G.C.Ireton, C.Knoeber, B.L.Stoddard, M.E.Black. Random Mutagenesis and Selection of Escherichia Coli Cytosine Deaminase For Cancer Gene Therapy. Protein Eng.Des.Sel. V. 17 625 2004.
ISSN: ISSN 1741-0126
PubMed: 15381761
DOI: 10.1093/PROTEIN/GZH074
Page generated: Wed Jul 16 20:18:43 2025

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