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Zinc 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:

Iron (Fe) 2 atoms

Zinc Binding Sites:

The binding sites of Zinc 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 Zinc atom.
In total 2 binding sites of Zinc 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 Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in 1hxq

Go back to Zinc Binding Sites List in 1hxq
Zinc 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 Zinc with other atoms in the Zn 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:Zn350

b:18.9
occ:1.00
 ND1 A:HIS164 1.8 14.2 1.0
ND1 A:HIS115 2.0 20.1 1.0
SG A:CYS52 2.2 15.1 1.0
SG A:CYS55 2.3 19.1 1.0
CE1 A:HIS164 2.7 23.2 1.0
CE1 A:HIS115 2.8 10.4 1.0
CB A:CYS52 2.9 15.4 1.0
CG A:HIS164 2.9 11.8 1.0
CG A:HIS115 3.1 31.4 1.0
CB A:CYS55 3.3 12.5 1.0
CB A:HIS164 3.4 24.0 1.0
N A:CYS55 3.5 12.6 1.0
CA A:CYS55 3.7 10.4 1.0
CB A:HIS115 3.7 19.5 1.0
NE2 A:HIS164 3.9 15.9 1.0
NE2 A:HIS115 4.0 15.2 1.0
CD2 A:HIS164 4.0 8.5 1.0
CD2 A:HIS115 4.1 16.8 1.0
CA A:HIS115 4.1 5.4 1.0
C A:LEU54 4.2 8.6 1.0
CA A:CYS52 4.3 22.3 1.0
CA A:HIS164 4.4 10.0 1.0
CB A:ASP49 4.5 25.5 1.0
CB A:LEU54 4.6 10.7 1.0
O A:LEU54 4.7 14.6 1.0
CA A:LEU54 4.7 10.0 1.0
C A:CYS52 4.8 20.4 1.0
N A:ASP49 4.8 15.1 1.0
N A:LEU54 4.8 16.6 1.0
O A:CYS52 4.9 16.9 1.0
O A:ASP49 4.9 31.7 1.0
OD1 A:ASN162 4.9 46.7 1.0
N A:HIS115 5.0 15.6 1.0

Zinc binding site 2 out of 2 in 1hxq

Go back to Zinc Binding Sites List in 1hxq
Zinc 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 Zinc with other atoms in the Zn 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:Zn350

b:20.4
occ:1.00
 ND1 B:HIS115 1.7 30.8 1.0
ND1 B:HIS164 1.7 15.7 1.0
SG B:CYS52 2.2 16.6 1.0
SG B:CYS55 2.2 18.4 1.0
CE1 B:HIS164 2.6 17.9 1.0
CE1 B:HIS115 2.6 29.4 1.0
CG B:HIS115 2.8 20.0 1.0
CG B:HIS164 2.9 11.2 1.0
CB B:CYS52 2.9 15.8 1.0
CB B:CYS55 3.3 13.9 1.0
CB B:HIS115 3.4 14.3 1.0
N B:CYS55 3.5 14.7 1.0
CB B:HIS164 3.5 25.2 1.0
CA B:CYS55 3.6 18.3 1.0
NE2 B:HIS164 3.8 14.4 1.0
NE2 B:HIS115 3.8 27.3 1.0
CD2 B:HIS115 3.9 26.1 1.0
CD2 B:HIS164 3.9 18.5 1.0
C B:LEU54 4.0 11.1 1.0
CA B:HIS115 4.1 12.3 1.0
CA B:CYS52 4.3 15.8 1.0
CA B:HIS164 4.4 10.6 1.0
O B:LEU54 4.4 15.4 1.0
CB B:LEU54 4.5 13.5 1.0
CA B:LEU54 4.6 11.0 1.0
O B:HOH469 4.7 23.4 1.0
N B:LEU54 4.7 14.4 1.0
N B:ASP49 4.7 23.0 1.0
OD1 B:ASN162 4.7 45.2 1.0
C B:CYS52 4.7 24.7 1.0
O B:CYS52 4.8 20.9 1.0
CB B:ASP49 4.8 24.5 1.0
N B:HIS115 5.0 8.8 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: Sun Oct 13 02:37:58 2024

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