Zinc in PDB 5gk8: Structure of E.Coli Fructose 1,6-Bisphosphate Aldolase, Acetate Bound Form

All present enzymatic activity of Structure of E.Coli Fructose 1,6-Bisphosphate Aldolase, Acetate Bound Form:
4.1.2.13;

The structure of Structure of E.Coli Fructose 1,6-Bisphosphate Aldolase, Acetate Bound Form, PDB code: 5gk8 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)	36.61 / 2.00
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	66.598, 73.351, 78.269, 90.00, 102.63, 90.00
R / Rfree (%)	16.1 / 20

The binding sites of Zinc atom in the Structure of E.Coli Fructose 1,6-Bisphosphate Aldolase, Acetate Bound Form (pdb code 5gk8). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 4 binding sites of Zinc where determined in the Structure of E.Coli Fructose 1,6-Bisphosphate Aldolase, Acetate Bound Form, PDB code: 5gk8:
Jump to Zinc binding site number: 1; 2; 3; 4;

Zinc binding site 1 out of 4 in the Structure of E.Coli Fructose 1,6-Bisphosphate Aldolase, Acetate Bound Form


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Structure of E.Coli Fructose 1,6-Bisphosphate Aldolase, Acetate Bound Form within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn405 b:26.5 occ:0.71 OE1 A:GLU174 2.3 24.8 1.0 CE1 A:HIS110 2.3 23.4 1.0 NE2 A:HIS226 2.3 36.4 1.0 OE2 A:GLU174 2.4 32.2 1.0 ND1 A:HIS264 2.6 32.5 1.0 CD A:GLU174 2.6 24.4 1.0 O A:HOH509 2.7 29.3 1.0 CD2 A:HIS226 3.1 37.8 1.0 NE2 A:HIS110 3.1 24.1 1.0 ND1 A:HIS110 3.3 28.0 1.0 CE1 A:HIS226 3.4 37.2 1.0 CE1 A:HIS264 3.4 31.1 1.0 CG A:HIS264 3.7 26.9 1.0 ZN A:ZN406 3.7 32.8 0.6 CB A:HIS264 4.0 22.6 1.0 O A:HOH540 4.0 35.4 1.0 CG A:GLU174 4.1 21.4 1.0 O A:HOH653 4.1 44.0 1.0 OD2 A:ASP144 4.2 24.4 1.0 CG A:HIS226 4.3 40.5 1.0 CD2 A:HIS110 4.3 22.8 1.0 ND1 A:HIS226 4.4 43.0 1.0 CG A:HIS110 4.4 26.8 1.0 NE2 A:HIS264 4.6 18.2 1.0 CD2 A:HIS264 4.7 24.1 1.0 CG A:ASP144 4.8 25.1 1.0 CB A:GLU174 4.9 18.3 1.0

Zinc binding site 2 out of 4 in the Structure of E.Coli Fructose 1,6-Bisphosphate Aldolase, Acetate Bound Form


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Structure of E.Coli Fructose 1,6-Bisphosphate Aldolase, Acetate Bound Form within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn406 b:32.8 occ:0.58 NE2 A:HIS110 2.0 24.1 1.0 O A:HOH645 2.4 35.6 1.0 O A:HOH521 2.6 27.0 1.0 O A:HOH655 2.9 45.1 1.0 CD2 A:HIS110 3.0 22.8 1.0 ND1 A:HIS264 3.0 32.5 1.0 CE1 A:HIS110 3.1 23.4 1.0 CG A:HIS264 3.3 26.9 1.0 CB A:HIS264 3.5 22.6 1.0 CD2 A:HIS226 3.6 37.8 1.0 CE1 A:HIS264 3.7 31.1 1.0 ZN A:ZN405 3.7 26.5 0.7 ND2 A:ASN286 4.1 16.8 1.0 CG A:HIS110 4.1 26.8 1.0 ND1 A:HIS110 4.1 28.0 1.0 NE2 A:HIS226 4.2 36.4 1.0 CD2 A:HIS264 4.2 24.1 1.0 OD2 A:ASP109 4.4 24.9 1.0 OD1 A:ASP109 4.4 24.4 1.0 NE2 A:HIS264 4.4 18.2 1.0 CA A:HIS264 4.4 24.6 1.0 CG A:HIS226 4.5 40.5 1.0 N A:GLY265 4.8 31.4 1.0 CG A:ASP109 4.8 22.8 1.0 CG A:ASN286 4.9 21.0 1.0 CB A:ASN286 5.0 18.0 1.0

Zinc binding site 3 out of 4 in the Structure of E.Coli Fructose 1,6-Bisphosphate Aldolase, Acetate Bound Form


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of Structure of E.Coli Fructose 1,6-Bisphosphate Aldolase, Acetate Bound Form within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn404 b:28.6 occ:0.67 CE1 B:HIS110 2.1 23.0 1.0 OE1 B:GLU174 2.2 26.7 1.0 NE2 B:HIS226 2.3 38.2 1.0 OE2 B:GLU174 2.5 31.1 1.0 O B:HOH543 2.5 25.9 1.0 CD B:GLU174 2.7 28.9 1.0 NE2 B:HIS110 2.9 27.4 1.0 ND1 B:HIS264 3.1 36.9 1.0 CD2 B:HIS226 3.2 42.2 1.0 ND1 B:HIS110 3.2 25.6 1.0 CE1 B:HIS226 3.3 40.8 1.0 ZN B:ZN405 3.7 30.8 0.6 CG B:HIS264 3.7 31.5 1.0 CE1 B:HIS264 3.7 34.5 1.0 CB B:HIS264 4.0 26.8 1.0 O B:HOH545 4.1 33.8 1.0 OD2 B:ASP144 4.1 28.2 1.0 CG B:GLU174 4.1 22.9 1.0 CD2 B:HIS110 4.2 19.9 1.0 CE B:MET142 4.2 33.4 1.0 CG B:HIS110 4.3 26.5 1.0 CG B:HIS226 4.3 41.2 1.0 ND1 B:HIS226 4.3 44.2 1.0 NE2 B:HIS264 4.5 24.7 1.0 CD2 B:HIS264 4.5 28.3 1.0 CG B:ASP144 4.7 27.0 1.0 CB B:GLU174 4.8 18.3 1.0

Zinc binding site 4 out of 4 in the Structure of E.Coli Fructose 1,6-Bisphosphate Aldolase, Acetate Bound Form


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 4 of Structure of E.Coli Fructose 1,6-Bisphosphate Aldolase, Acetate Bound Form within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn405 b:30.8 occ:0.60 NE2 B:HIS110 2.0 27.4 1.0 ND1 B:HIS264 2.4 36.9 1.0 O B:HOH658 2.4 38.3 1.0 O B:HOH640 2.5 33.9 1.0 O B:HOH531 2.6 25.7 1.0 CD2 B:HIS110 2.9 19.9 1.0 CE1 B:HIS110 3.1 23.0 1.0 CG B:HIS264 3.2 31.5 1.0 CB B:HIS264 3.4 26.8 1.0 CE1 B:HIS264 3.4 34.5 1.0 CD2 B:HIS226 3.6 42.2 1.0 ZN B:ZN404 3.7 28.6 0.7 NE2 B:HIS226 4.1 38.2 1.0 CG B:HIS110 4.1 26.5 1.0 ND1 B:HIS110 4.2 25.6 1.0 ND2 B:ASN286 4.2 22.4 1.0 CA B:HIS264 4.3 24.6 1.0 CG B:HIS226 4.3 41.2 1.0 CD2 B:HIS264 4.4 28.3 1.0 OD2 B:ASP109 4.4 23.7 1.0 NE2 B:HIS264 4.4 24.7 1.0 OD1 B:ASP109 4.4 21.3 1.0 N B:GLY265 4.6 29.9 1.0 CG B:ASP109 4.9 25.4 1.0 CB B:HIS226 4.9 46.6 1.0 CE1 B:HIS226 4.9 40.8 1.0 C B:HIS264 4.9 28.9 1.0

T.H.Tran, K.H.Huynh, T.H.Ho, L.W.Kang. Structure of E.Coli Fructose 1,6-Bisphosphate Aldolase, Acetate Bound Form To Be Published.