Atomistry » Iron » PDB 1qov-1ra5 » 1ra0
Atomistry »
  Iron »
    PDB 1qov-1ra5 »
      1ra0 »

Iron in PDB 1ra0: Bacterial Cytosine Deaminase D314G Mutant Bound to 5-Fluoro-4-(S)- Hydroxy-3,4-Dihydropyrimidine.

Enzymatic activity of Bacterial Cytosine Deaminase D314G Mutant Bound to 5-Fluoro-4-(S)- Hydroxy-3,4-Dihydropyrimidine.

All present enzymatic activity of Bacterial Cytosine Deaminase D314G Mutant Bound to 5-Fluoro-4-(S)- Hydroxy-3,4-Dihydropyrimidine.:
3.5.4.1;

Protein crystallography data

The structure of Bacterial Cytosine Deaminase D314G Mutant Bound to 5-Fluoro-4-(S)- Hydroxy-3,4-Dihydropyrimidine., PDB code: 1ra0 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) 20.00 / 1.12
Space group H 3 2
Cell size a, b, c (Å), α, β, γ (°) 109.257, 109.257, 240.842, 90.00, 90.00, 120.00
R / Rfree (%) 16.8 / 17.2

Other elements in 1ra0:

The structure of Bacterial Cytosine Deaminase D314G Mutant Bound to 5-Fluoro-4-(S)- Hydroxy-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 D314G Mutant Bound to 5-Fluoro-4-(S)- Hydroxy-3,4-Dihydropyrimidine. (pdb code 1ra0). 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 D314G Mutant Bound to 5-Fluoro-4-(S)- Hydroxy-3,4-Dihydropyrimidine., PDB code: 1ra0:

Iron binding site 1 out of 1 in 1ra0

Go back to Iron Binding Sites List in 1ra0
Iron binding site 1 out of 1 in the Bacterial Cytosine Deaminase D314G Mutant Bound to 5-Fluoro-4-(S)- Hydroxy-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 D314G Mutant Bound to 5-Fluoro-4-(S)- Hydroxy-3,4-Dihydropyrimidine. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe500

b:7.4
occ:0.90
 NE2 A:HIS63 2.0 6.7 1.0
NE2 A:HIS61 2.1 6.1 1.0
O4 A:FPY501 2.1 11.3 0.9
NE2 A:HIS214 2.3 7.2 1.0
OD2 A:ASP313 2.5 10.7 1.0
CE1 A:HIS61 3.0 6.0 1.0
CE1 A:HIS63 3.0 6.6 1.0
CD2 A:HIS63 3.1 5.8 1.0
CD2 A:HIS61 3.1 5.1 1.0
CE1 A:HIS214 3.2 6.6 1.0
CD2 A:HIS214 3.3 6.5 1.0
C4 A:FPY501 3.3 8.3 0.9
C5 A:FPY501 3.4 13.6 0.9
CG A:ASP313 3.4 8.1 1.0
OD1 A:ASP313 3.6 8.0 1.0
NE2 A:HIS246 3.7 6.9 1.0
F5 A:FPY501 3.7 10.1 1.0
N3 A:FPY501 3.8 8.9 0.9
C6 A:FPY501 3.8 11.7 0.9
ND1 A:HIS63 4.1 6.4 1.0
ND1 A:HIS61 4.1 5.4 1.0
CG A:HIS63 4.2 5.8 1.0
CG A:HIS61 4.2 4.6 1.0
N1 A:FPY501 4.2 12.2 0.9
C2 A:FPY501 4.3 11.3 0.9
ND1 A:HIS214 4.3 5.8 1.0
CG A:HIS214 4.4 5.5 1.0
CE1 A:HIS246 4.6 8.1 1.0
CD2 A:HIS246 4.6 7.3 1.0
CB A:ASP313 4.8 6.3 1.0
CD2 A:HIS122 4.8 5.9 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: Sat Aug 3 14:03:07 2024

Last articles

Zn in 9JYW
Zn in 9IR4
Zn in 9IR3
Zn in 9GMX
Zn in 9GMW
Zn in 9JEJ
Zn in 9ERF
Zn in 9ERE
Zn in 9EGV
Zn in 9EGW
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy