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Iron in PDB 1k70: The Structure of Escherichia Coli Cytosine Deaminase Bound to 4- Hydroxy-3,4-Dihydro-1H-Pyrimidin-2-One

Enzymatic activity of The Structure of Escherichia Coli Cytosine Deaminase Bound to 4- Hydroxy-3,4-Dihydro-1H-Pyrimidin-2-One

All present enzymatic activity of The Structure of Escherichia Coli Cytosine Deaminase Bound to 4- Hydroxy-3,4-Dihydro-1H-Pyrimidin-2-One:
3.5.4.1;

Protein crystallography data

The structure of The Structure of Escherichia Coli Cytosine Deaminase Bound to 4- Hydroxy-3,4-Dihydro-1H-Pyrimidin-2-One, PDB code: 1k70 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) 19.97 / 1.80
Space group H 3 2
Cell size a, b, c (Å), α, β, γ (°) 109.500, 109.500, 240.400, 90.00, 90.00, 120.00
R / Rfree (%) 17.6 / 20.1

Iron Binding Sites:

The binding sites of Iron atom in the The Structure of Escherichia Coli Cytosine Deaminase Bound to 4- Hydroxy-3,4-Dihydro-1H-Pyrimidin-2-One (pdb code 1k70). 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 Bound to 4- Hydroxy-3,4-Dihydro-1H-Pyrimidin-2-One, PDB code: 1k70:

Iron binding site 1 out of 1 in 1k70

Go back to Iron Binding Sites List in 1k70
Iron binding site 1 out of 1 in the The Structure of Escherichia Coli Cytosine Deaminase Bound to 4- Hydroxy-3,4-Dihydro-1H-Pyrimidin-2-One


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 Bound to 4- Hydroxy-3,4-Dihydro-1H-Pyrimidin-2-One within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe502

b:19.0
occ:0.90
 NE2 A:HIS61 2.1 11.0 1.0
NE2 A:HIS63 2.1 9.1 1.0
O4 A:HPY501 2.1 16.1 0.9
NE2 A:HIS214 2.4 11.6 1.0
OD2 A:ASP313 2.5 10.1 1.0
CD2 A:HIS63 3.0 12.4 1.0
CE1 A:HIS61 3.1 11.4 1.0
CD2 A:HIS61 3.1 11.0 1.0
CE1 A:HIS63 3.2 13.8 1.0
CE1 A:HIS214 3.2 12.2 1.0
C5 A:HPY501 3.3 18.5 0.9
C4 A:HPY501 3.3 17.4 0.9
CD2 A:HIS214 3.3 11.8 1.0
CG A:ASP313 3.4 13.0 1.0
OD1 A:ASP313 3.6 12.5 1.0
NE2 A:HIS246 3.7 8.2 1.0
C6 A:HPY501 3.8 19.9 0.9
N3 A:HPY501 3.8 15.4 0.9
CG A:HIS63 4.2 11.2 1.0
ND1 A:HIS61 4.2 9.3 1.0
ND1 A:HIS63 4.2 10.3 1.0
CG A:HIS61 4.2 10.3 1.0
N1 A:HPY501 4.3 18.4 0.9
C2 A:HPY501 4.3 19.9 0.9
ND1 A:HIS214 4.4 12.0 1.0
CG A:HIS214 4.4 12.1 1.0
CD2 A:HIS246 4.6 8.0 1.0
CE1 A:HIS246 4.6 9.9 1.0
CB A:ASP313 4.7 10.4 1.0
ND1 A:HIS122 4.8 13.2 1.0

Reference:

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
Page generated: Sat Aug 3 09:07:24 2024

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