Iron in PDB 1hxp: Nucleotide Transferase

All present enzymatic activity of Nucleotide Transferase:
2.7.7.10;

The structure of Nucleotide Transferase, PDB code: 1hxp was solved by J.E.Wedekind, P.A.Frey, I.Rayment, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	50.00 / 1.80
Space group	P 21 21 2
Cell size a, b, c (Å), α, β, γ (°)	58.600, 217.200, 69.600, 90.00, 90.00, 90.00
R / Rfree (%)	n/a / n/a

The structure of Nucleotide Transferase also contains other interesting chemical elements:

Zinc

(Zn)

2 atoms

The binding sites of Iron atom in the Nucleotide Transferase (pdb code 1hxp). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the Nucleotide Transferase, PDB code: 1hxp:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the Nucleotide Transferase


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Nucleotide Transferase within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe351 b:11.4 occ:1.00 OE2 A:GLU182 1.8 10.3 1.0 NE2 A:HIS298 2.0 9.6 1.0 ND1 A:HIS281 2.0 11.6 1.0 NE2 A:HIS296 2.0 4.7 1.0 OE1 A:GLU182 2.3 14.9 1.0 CD A:GLU182 2.4 10.0 1.0 CE1 A:HIS296 2.9 9.7 1.0 CE1 A:HIS281 3.0 15.4 1.0 CE1 A:HIS298 3.0 3.7 1.0 CD2 A:HIS298 3.0 5.3 1.0 CD2 A:HIS296 3.1 8.3 1.0 CG A:HIS281 3.1 10.9 1.0 CB A:HIS281 3.5 7.9 1.0 CG A:GLU182 3.9 12.4 1.0 NE2 A:HIS281 4.1 14.5 1.0 ND1 A:HIS296 4.1 7.8 1.0 ND1 A:HIS298 4.1 5.8 1.0 CD2 A:HIS281 4.1 16.4 1.0 CG A:HIS296 4.2 6.4 1.0 CG A:HIS298 4.2 6.1 1.0 CD1 A:LEU17 4.3 10.2 1.0 O A:HOH418 4.5 63.1 1.0 CB A:GLU182 4.9 3.7 1.0 CA A:HIS281 4.9 5.4 1.0

Iron binding site 2 out of 2 in the Nucleotide Transferase


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Nucleotide Transferase within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe350 b:12.9 occ:1.00 OE2 B:GLU182 1.9 14.8 1.0 ND1 B:HIS281 2.0 13.3 1.0 NE2 B:HIS298 2.0 10.1 1.0 NE2 B:HIS296 2.1 8.9 1.0 OE1 B:GLU182 2.3 15.6 1.0 CD B:GLU182 2.4 18.9 1.0 CE1 B:HIS298 3.0 8.8 1.0 CE1 B:HIS281 3.0 18.5 1.0 CD2 B:HIS296 3.0 10.9 1.0 CD2 B:HIS298 3.1 6.2 1.0 CG B:HIS281 3.1 17.2 1.0 CE1 B:HIS296 3.1 12.0 1.0 CB B:HIS281 3.5 11.1 1.0 CG B:GLU182 3.9 13.7 1.0 ND1 B:HIS298 4.1 9.4 1.0 NE2 B:HIS281 4.1 14.6 1.0 CD2 B:HIS281 4.2 17.8 1.0 CG B:HIS296 4.2 9.8 1.0 CG B:HIS298 4.2 9.1 1.0 ND1 B:HIS296 4.2 11.2 1.0 O B:HOH502 4.2 39.8 1.0 CD1 B:LEU17 4.3 12.4 1.0 CB B:GLU182 4.9 10.9 1.0 CA B:HIS281 5.0 11.7 1.0

J.E.Wedekind, P.A.Frey, I.Rayment. Three-Dimensional Structure of Galactose-1-Phosphate Uridylyltransferase From Escherichia Coli at 1.8 A Resolution. Biochemistry V. 34 11049 1995.
ISSN: ISSN 0006-2960
PubMed: 7669762
DOI: 10.1021/BI00035A010