Zinc in PDB 3gak: Structure of Giardia Fructose-1,6-Biphosphate Aldolase

All present enzymatic activity of Structure of Giardia Fructose-1,6-Biphosphate Aldolase:
4.1.2.13;

The structure of Structure of Giardia Fructose-1,6-Biphosphate Aldolase, PDB code: 3gak was solved by A.Galkin, O.Herzberg, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	10.00 / 2.90
Space group	P 61
Cell size a, b, c (Å), α, β, γ (°)	62.920, 62.920, 318.590, 90.00, 90.00, 120.00
R / Rfree (%)	22 / 28.6

The binding sites of Zinc atom in the Structure of Giardia Fructose-1,6-Biphosphate Aldolase (pdb code 3gak). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Structure of Giardia Fructose-1,6-Biphosphate Aldolase, PDB code: 3gak:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Structure of Giardia Fructose-1,6-Biphosphate Aldolase


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Structure of Giardia Fructose-1,6-Biphosphate Aldolase within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn331 b:44.5 occ:1.00 ND1 A:HIS210 2.0 48.7 1.0 OE2 A:GLU135 2.2 58.5 1.0 CE1 A:HIS210 2.8 48.7 1.0 CD A:GLU135 2.9 58.5 1.0 OE1 A:GLU135 3.1 58.5 1.0 CE A:MET103 3.2 61.0 1.0 NE2 A:HIS84 3.2 56.7 1.0 CG A:HIS210 3.2 48.7 1.0 CD2 A:HIS84 3.7 56.7 1.0 CB A:HIS210 3.7 47.2 1.0 NE2 A:HIS210 4.0 48.7 1.0 CD2 A:HIS210 4.2 48.7 1.0 CG A:GLU135 4.2 58.5 1.0 SD A:MET103 4.3 61.0 1.0 CE1 A:HIS84 4.3 56.7 1.0 OD2 A:ASP105 4.3 54.9 1.0 CB A:GLU135 4.6 82.7 1.0 CB A:ALA171 4.8 48.1 1.0 CG A:ASP105 4.9 54.9 1.0 CG A:HIS84 4.9 56.7 1.0

Zinc binding site 2 out of 2 in the Structure of Giardia Fructose-1,6-Biphosphate Aldolase


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Structure of Giardia Fructose-1,6-Biphosphate Aldolase within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn332 b:44.5 occ:1.00 NE2 B:HIS84 2.2 70.4 1.0 ND1 B:HIS210 2.3 39.7 1.0 NE2 B:HIS178 2.8 95.3 1.0 CG B:HIS210 3.0 39.7 1.0 CE1 B:HIS84 3.1 70.4 1.0 CD2 B:HIS84 3.1 70.4 1.0 CE1 B:HIS210 3.3 39.7 1.0 CB B:HIS210 3.3 28.9 1.0 CE1 B:HIS178 3.3 95.3 1.0 CD2 B:HIS178 4.0 95.3 1.0 ND1 B:HIS84 4.1 70.4 1.0 CD2 B:HIS210 4.1 39.7 1.0 CG B:HIS84 4.1 70.4 1.0 NE2 B:HIS210 4.2 39.7 1.0 ND1 B:HIS178 4.5 95.3 1.0 OE1 B:GLU135 4.5 54.6 1.0 CA B:HIS210 4.7 28.9 1.0 CE B:MET103 4.8 34.6 1.0 CG B:HIS178 4.8 95.3 1.0 OD2 B:ASP83 5.0 32.9 1.0

A.Galkin, Z.Li, L.Li, L.Kulakova, L.R.Pal, D.Dunaway-Mariano, O.Herzberg. Structural Insights Into the Substrate Binding and Stereoselectivity of Giardia Fructose-1,6-Bisphosphate Aldolase. Biochemistry V. 48 3186 2009.
ISSN: ISSN 0006-2960
PubMed: 19236002
DOI: 10.1021/BI9001166