Iron in PDB 1k6w: The Structure of Escherichia Coli Cytosine Deaminase

All present enzymatic activity of The Structure of Escherichia Coli Cytosine Deaminase:
3.5.4.1;

The structure of The Structure of Escherichia Coli Cytosine Deaminase, PDB code: 1k6w was solved by G.C.Ireton, G.Mcdermott, M.E.Black, B.L.Stoddard, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	19.98 / 1.75
Space group	H 3 2
Cell size a, b, c (Å), α, β, γ (°)	109.150, 109.150, 240.050, 90.00, 90.00, 120.00
R / Rfree (%)	15.5 / 17.2

The binding sites of Iron atom in the The Structure of Escherichia Coli Cytosine Deaminase (pdb code 1k6w). 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 The Structure of Escherichia Coli Cytosine Deaminase, PDB code: 1k6w:

Iron binding site 1 out of 1 in the The Structure of Escherichia Coli Cytosine Deaminase


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of The Structure of Escherichia Coli Cytosine Deaminase within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe501 b:10.8 occ:0.97 O A:HOH1000 1.9 7.7 1.0 NE2 A:HIS63 2.1 5.0 1.0 NE2 A:HIS61 2.1 3.7 1.0 NE2 A:HIS214 2.2 6.3 1.0 OD2 A:ASP313 2.6 6.6 1.0 CD2 A:HIS63 3.0 6.8 1.0 CE1 A:HIS61 3.0 4.3 1.0 CE1 A:HIS63 3.1 7.7 1.0 CD2 A:HIS61 3.1 4.0 1.0 CE1 A:HIS214 3.2 5.1 1.0 CD2 A:HIS214 3.2 6.1 1.0 CG A:ASP313 3.6 8.7 1.0 NE2 A:HIS246 3.8 4.4 1.0 O A:HOH742 3.8 24.1 1.0 OD1 A:ASP313 3.8 8.5 1.0 CG A:HIS63 4.2 6.1 1.0 ND1 A:HIS61 4.2 4.2 1.0 ND1 A:HIS63 4.2 5.4 1.0 CG A:HIS61 4.2 2.4 1.0 ND1 A:HIS214 4.3 7.4 1.0 O A:HOH740 4.3 19.3 1.0 CG A:HIS214 4.3 5.4 1.0 O A:HOH888 4.4 22.5 1.0 CD2 A:HIS246 4.6 4.6 1.0 ND1 A:HIS122 4.7 8.0 1.0 CE1 A:HIS246 4.7 5.6 1.0 CB A:ASP313 4.9 7.5 1.0 CG A:HIS122 4.9 4.1 1.0

G.C.Ireton, G.Mcdermott, M.E.Black, B.L.Stoddard. The Structure of Escherichia Coli Cytosine Deaminase. J.Mol.Biol. V. 315 687 2002.
ISSN: ISSN 0022-2836
PubMed: 11812140
DOI: 10.1006/JMBI.2001.5277