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Iron in PDB 1hxq: The Structure of Nucleotidylated Galactose-1-Phosphate Uridylyltransferase From Escherichia Coli at 1.86 Angstroms Resolution

Enzymatic activity of The Structure of Nucleotidylated Galactose-1-Phosphate Uridylyltransferase From Escherichia Coli at 1.86 Angstroms Resolution

All present enzymatic activity of The Structure of Nucleotidylated Galactose-1-Phosphate Uridylyltransferase From Escherichia Coli at 1.86 Angstroms Resolution:
2.7.7.12;

Protein crystallography data

The structure of The Structure of Nucleotidylated Galactose-1-Phosphate Uridylyltransferase From Escherichia Coli at 1.86 Angstroms Resolution, PDB code: 1hxq 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) 65.00 / 1.86
Space group P 21 21 2
Cell size a, b, c (Å), α, β, γ (°) 57.200, 215.400, 68.900, 90.00, 90.00, 90.00
R / Rfree (%) 19.6 / n/a

Other elements in 1hxq:

The structure of The Structure of Nucleotidylated Galactose-1-Phosphate Uridylyltransferase From Escherichia Coli at 1.86 Angstroms Resolution also contains other interesting chemical elements:

Zinc (Zn) 2 atoms

Iron Binding Sites:

The binding sites of Iron atom in the The Structure of Nucleotidylated Galactose-1-Phosphate Uridylyltransferase From Escherichia Coli at 1.86 Angstroms Resolution (pdb code 1hxq). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the The Structure of Nucleotidylated Galactose-1-Phosphate Uridylyltransferase From Escherichia Coli at 1.86 Angstroms Resolution, PDB code: 1hxq:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in 1hxq

Go back to Iron Binding Sites List in 1hxq
Iron binding site 1 out of 2 in the The Structure of Nucleotidylated Galactose-1-Phosphate Uridylyltransferase From Escherichia Coli at 1.86 Angstroms Resolution


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 Nucleotidylated Galactose-1-Phosphate Uridylyltransferase From Escherichia Coli at 1.86 Angstroms Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe351

b:22.6
occ:1.00
 NE2 A:HIS298 2.0 4.8 1.0
ND1 A:HIS281 2.0 15.0 1.0
OE2 A:GLU182 2.1 17.8 1.0
NE2 A:HIS296 2.1 7.2 1.0
OE1 A:GLU182 2.2 12.5 1.0
CD A:GLU182 2.5 17.6 1.0
CE1 A:HIS281 2.9 13.1 1.0
CE1 A:HIS298 3.0 5.0 1.0
CD2 A:HIS298 3.0 4.7 1.0
CD2 A:HIS296 3.0 5.2 1.0
CG A:HIS281 3.1 15.5 1.0
CE1 A:HIS296 3.2 5.4 1.0
CB A:HIS281 3.5 17.9 1.0
CG A:GLU182 4.0 13.2 1.0
O A:HOH356 4.1 41.5 1.0
NE2 A:HIS281 4.1 23.2 1.0
ND1 A:HIS298 4.1 4.2 1.0
CG A:HIS298 4.1 5.2 1.0
CD2 A:HIS281 4.1 18.6 1.0
CG A:HIS296 4.2 2.7 1.0
CD1 A:LEU17 4.2 3.9 1.0
ND1 A:HIS296 4.3 8.1 1.0
CB A:GLU182 4.9 6.7 1.0
CA A:HIS281 5.0 4.7 1.0

Iron binding site 2 out of 2 in 1hxq

Go back to Iron Binding Sites List in 1hxq
Iron binding site 2 out of 2 in the The Structure of Nucleotidylated Galactose-1-Phosphate Uridylyltransferase From Escherichia Coli at 1.86 Angstroms Resolution


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of The Structure of Nucleotidylated Galactose-1-Phosphate Uridylyltransferase From Escherichia Coli at 1.86 Angstroms Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe351

b:22.9
occ:1.00
 OE2 B:GLU182 1.9 29.0 1.0
NE2 B:HIS296 2.1 9.7 1.0
ND1 B:HIS281 2.1 12.7 1.0
NE2 B:HIS298 2.1 8.5 1.0
OE1 B:GLU182 2.2 16.2 1.0
CD B:GLU182 2.3 11.0 1.0
CD2 B:HIS296 3.0 8.1 1.0
CE1 B:HIS298 3.0 10.8 1.0
CE1 B:HIS281 3.1 14.2 1.0
CG B:HIS281 3.2 10.9 1.0
CE1 B:HIS296 3.2 16.6 1.0
CD2 B:HIS298 3.2 8.3 1.0
CB B:HIS281 3.5 13.4 1.0
CG B:GLU182 3.7 13.8 1.0
O B:HOH358 3.9 20.9 1.0
CG B:HIS296 4.2 7.6 1.0
ND1 B:HIS298 4.2 8.2 1.0
NE2 B:HIS281 4.2 7.1 1.0
ND1 B:HIS296 4.2 11.3 1.0
CD2 B:HIS281 4.3 12.1 1.0
CD1 B:LEU17 4.3 13.3 1.0
CG B:HIS298 4.3 6.7 1.0
O B:HOH398 4.4 26.4 1.0
CB B:GLU182 4.8 17.3 1.0
CD2 B:LEU17 5.0 9.7 1.0
CA B:HIS281 5.0 6.1 1.0

Reference:

J.E.Wedekind, P.A.Frey, I.Rayment. The Structure of Nucleotidylated Histidine-166 of Galactose-1-Phosphate Uridylyltransferase Provides Insight Into Phosphoryl Group Transfer. Biochemistry V. 35 11560 1996.
ISSN: ISSN 0006-2960
PubMed: 8794735
DOI: 10.1021/BI9612677
Page generated: Sat Aug 3 07:53:28 2024

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