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Zinc in PDB 5gk3: Native Structure of Fructose 1,6-Bisphosphate Aldolase From Escherichia Coli at 1.8 Angstrom Resolution

Enzymatic activity of Native Structure of Fructose 1,6-Bisphosphate Aldolase From Escherichia Coli at 1.8 Angstrom Resolution

All present enzymatic activity of Native Structure of Fructose 1,6-Bisphosphate Aldolase From Escherichia Coli at 1.8 Angstrom Resolution:
4.1.2.13;

Protein crystallography data

The structure of Native Structure of Fructose 1,6-Bisphosphate Aldolase From Escherichia Coli at 1.8 Angstrom Resolution, PDB code: 5gk3 was solved by T.H.Tran, K.H.Huynh, T.H.Ho, L.W.Kang, 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 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 72.251, 72.837, 73.361, 90.00, 103.09, 90.00
R / Rfree (%) 15.5 / 18.9

Zinc Binding Sites:

The binding sites of Zinc atom in the Native Structure of Fructose 1,6-Bisphosphate Aldolase From Escherichia Coli at 1.8 Angstrom Resolution (pdb code 5gk3). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Native Structure of Fructose 1,6-Bisphosphate Aldolase From Escherichia Coli at 1.8 Angstrom Resolution, PDB code: 5gk3:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in 5gk3

Go back to Zinc Binding Sites List in 5gk3
Zinc binding site 1 out of 2 in the Native Structure of Fructose 1,6-Bisphosphate Aldolase From Escherichia Coli at 1.8 Angstrom Resolution


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Native Structure of Fructose 1,6-Bisphosphate Aldolase From Escherichia Coli at 1.8 Angstrom Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn402

b:22.1
occ:0.70
OE1 A:GLU174 2.1 25.2 1.0
NE2 A:HIS226 2.1 27.0 1.0
NE2 A:HIS110 2.2 20.4 1.0
OE2 A:GLU174 2.3 24.1 1.0
ND1 A:HIS264 2.3 26.4 1.0
O A:HOH617 2.3 26.2 1.0
CD A:GLU174 2.5 23.8 1.0
CE1 A:HIS264 3.0 28.0 1.0
CE1 A:HIS226 3.1 30.0 1.0
CE1 A:HIS110 3.1 24.8 1.0
CD2 A:HIS226 3.1 31.2 1.0
CD2 A:HIS110 3.1 20.6 1.0
CG A:HIS264 3.4 22.8 1.0
O A:HOH686 3.9 21.1 1.0
CB A:HIS264 3.9 21.6 1.0
CG A:GLU174 4.0 20.9 1.0
O A:HOH699 4.1 41.1 1.0
O A:HOH514 4.1 30.9 1.0
ND1 A:HIS226 4.2 33.7 1.0
NE2 A:HIS264 4.2 20.3 1.0
ND1 A:HIS110 4.2 23.2 1.0
CG A:HIS226 4.2 33.6 1.0
CG A:HIS110 4.3 19.9 1.0
OD2 A:ASP144 4.3 24.7 1.0
CD2 A:HIS264 4.4 22.1 1.0
CE A:MET142 4.5 37.9 1.0
CG A:ASP144 4.7 24.1 1.0
CB A:GLU174 4.8 20.7 1.0

Zinc binding site 2 out of 2 in 5gk3

Go back to Zinc Binding Sites List in 5gk3
Zinc binding site 2 out of 2 in the Native Structure of Fructose 1,6-Bisphosphate Aldolase From Escherichia Coli at 1.8 Angstrom Resolution


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Native Structure of Fructose 1,6-Bisphosphate Aldolase From Escherichia Coli at 1.8 Angstrom Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn404

b:17.8
occ:0.70
OE1 B:GLU174 2.1 20.8 1.0
NE2 B:HIS226 2.1 23.4 1.0
NE2 B:HIS110 2.1 17.5 1.0
ND1 B:HIS264 2.2 22.3 1.0
OE2 B:GLU174 2.3 20.4 1.0
O B:HOH635 2.3 25.8 1.0
CD B:GLU174 2.5 22.6 1.0
CD2 B:HIS226 3.0 26.5 1.0
CE1 B:HIS110 3.1 20.8 1.0
CE1 B:HIS264 3.1 22.8 1.0
CE1 B:HIS226 3.1 25.4 1.0
CD2 B:HIS110 3.1 19.4 1.0
CG B:HIS264 3.3 20.4 1.0
O B:HOH687 3.8 24.4 1.0
CB B:HIS264 3.8 19.5 1.0
CG B:GLU174 4.0 17.5 1.0
O B:HOH707 4.1 40.1 1.0
CG B:HIS226 4.2 30.9 1.0
ND1 B:HIS110 4.2 20.3 1.0
ND1 B:HIS226 4.2 27.4 1.0
NE2 B:HIS264 4.2 16.8 1.0
CG B:HIS110 4.3 18.6 1.0
OD2 B:ASP144 4.3 21.4 1.0
O B:HOH540 4.4 27.3 1.0
CD2 B:HIS264 4.4 18.6 1.0
CB B:GLU174 4.8 19.2 1.0
CG B:ASP144 4.8 20.4 1.0
CE B:MET142 4.9 30.5 1.0

Reference:

T.H.Tran, K.H.Huynh, T.H.Ho, L.W.Kang. Apo Structure of Fructose 1,6-Bisphosphate Aldolase From Escherichia Coli at 1.8 Angstrom Resolution To Be Published.
Page generated: Sun Oct 27 17:02:09 2024

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