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Zinc in PDB 7t85: Crystal Structure of the N-Terminal Domain of the Phosphate Acetyltransferase From Escherichia Coli

Enzymatic activity of Crystal Structure of the N-Terminal Domain of the Phosphate Acetyltransferase From Escherichia Coli

All present enzymatic activity of Crystal Structure of the N-Terminal Domain of the Phosphate Acetyltransferase From Escherichia Coli:
2.3.1.8;

Protein crystallography data

The structure of Crystal Structure of the N-Terminal Domain of the Phosphate Acetyltransferase From Escherichia Coli, PDB code: 7t85 was solved by Y.Kim, A.Dementiev, L.Welk, M.Endres, A.Joachimiak, Center For Structuralgenomics Of Infectious Diseases (Csgid), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 36.50 / 2.00
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 39.979, 56.66, 89.479, 90, 90, 90
R / Rfree (%) 19.9 / 23.3

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of the N-Terminal Domain of the Phosphate Acetyltransferase From Escherichia Coli (pdb code 7t85). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 3 binding sites of Zinc where determined in the Crystal Structure of the N-Terminal Domain of the Phosphate Acetyltransferase From Escherichia Coli, PDB code: 7t85:
Jump to Zinc binding site number: 1; 2; 3;

Zinc binding site 1 out of 3 in 7t85

Go back to Zinc Binding Sites List in 7t85
Zinc binding site 1 out of 3 in the Crystal Structure of the N-Terminal Domain of the Phosphate Acetyltransferase From Escherichia Coli


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Crystal Structure of the N-Terminal Domain of the Phosphate Acetyltransferase From Escherichia Coli within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn306

b:26.9
occ:0.88
OE2 A:GLU28 1.9 34.5 1.0
CD A:GLU28 2.7 30.6 1.0
OE1 A:GLU28 2.8 30.0 1.0
CG A:GLU28 4.1 27.1 1.0
O A:GLU28 4.6 27.7 1.0
O A:HOH440 4.8 53.6 1.0

Zinc binding site 2 out of 3 in 7t85

Go back to Zinc Binding Sites List in 7t85
Zinc binding site 2 out of 3 in the Crystal Structure of the N-Terminal Domain of the Phosphate Acetyltransferase From Escherichia Coli


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Crystal Structure of the N-Terminal Domain of the Phosphate Acetyltransferase From Escherichia Coli within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn307

b:24.6
occ:0.88
OE2 A:GLU89 1.8 23.9 1.0
OD1 A:ASP85 2.0 30.8 1.0
CG A:ASP85 2.8 29.3 1.0
CD A:GLU89 2.8 27.1 1.0
OD2 A:ASP85 2.9 36.4 1.0
CG A:GLU89 3.2 24.4 1.0
O A:HOH454 3.8 33.4 1.0
OE1 A:GLU89 3.9 30.1 1.0
CB A:ASP85 4.2 29.5 1.0
O2 A:EDO305 4.2 47.5 1.0
O A:ASP85 4.3 29.4 1.0
C2 A:EDO305 4.6 53.2 1.0
C A:ASP85 4.6 27.5 1.0
CB A:GLU89 4.7 25.1 1.0
CA A:ASP85 4.9 22.9 1.0

Zinc binding site 3 out of 3 in 7t85

Go back to Zinc Binding Sites List in 7t85
Zinc binding site 3 out of 3 in the Crystal Structure of the N-Terminal Domain of the Phosphate Acetyltransferase From Escherichia Coli


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of Crystal Structure of the N-Terminal Domain of the Phosphate Acetyltransferase From Escherichia Coli within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn308

b:37.3
occ:0.83
OE2 A:GLU76 2.0 47.0 1.0
O2 A:EDO302 2.1 39.6 1.0
O1 A:EDO302 2.2 38.4 1.0
NE2 A:HIS116 2.3 42.5 1.0
O A:HOH413 2.3 39.6 1.0
C1 A:EDO302 2.9 36.2 1.0
CD A:GLU76 2.9 31.1 1.0
C2 A:EDO302 2.9 42.0 1.0
CD2 A:HIS116 3.1 36.7 1.0
OE1 A:GLU76 3.1 36.0 1.0
CE1 A:HIS116 3.3 51.0 1.0
CG A:MSE72 3.9 42.2 1.0
CG A:HIS116 4.3 34.0 1.0
CG A:GLU76 4.3 29.2 1.0
ND1 A:HIS116 4.4 59.9 1.0
O A:HOH408 4.6 49.7 1.0
CB A:MSE72 4.9 38.9 1.0

Reference:

Y.Kim, A.Dementiev, L.Welk, M.Endres, A.Joachimiak, Center For Structural Genomics Of Infectious Diseases(Csgid). Crystal Structure of the N-Terminal Domain of the Phosphate Acetyltransferase From Escherichia Coli To Be Published.
Page generated: Thu Mar 31 05:24:36 2022

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