Zinc in PDB 2isv: Structure of Giardia Fructose-1,6-Biphosphate Aldolase in Complex with Phosphoglycolohydroxamate

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

The structure of Structure of Giardia Fructose-1,6-Biphosphate Aldolase in Complex with Phosphoglycolohydroxamate, PDB code: 2isv 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)	30.00 / 2.30
Space group	P 61
Cell size a, b, c (Å), α, β, γ (°)	62.360, 62.360, 319.860, 90.00, 90.00, 120.00
R / Rfree (%)	19.9 / 26.1

The binding sites of Zinc atom in the Structure of Giardia Fructose-1,6-Biphosphate Aldolase in Complex with Phosphoglycolohydroxamate (pdb code 2isv). 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 in Complex with Phosphoglycolohydroxamate, PDB code: 2isv:
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 in Complex with Phosphoglycolohydroxamate


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 in Complex with Phosphoglycolohydroxamate within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn326 b:69.0 occ:1.00 NE2 A:HIS84 2.2 58.4 1.0 ND1 A:HIS210 2.5 60.8 1.0 O1 A:PGH325 2.5 47.4 1.0 NE2 A:HIS178 2.5 99.0 1.0 O2 A:PGH325 2.5 39.8 1.0 C1 A:PGH325 3.1 62.3 1.0 CE1 A:HIS84 3.1 45.8 1.0 CD2 A:HIS84 3.2 52.7 1.0 CE1 A:HIS178 3.2 99.0 1.0 CG A:HIS210 3.3 52.2 1.0 N2 A:PGH325 3.4 61.2 1.0 CE1 A:HIS210 3.4 58.0 1.0 CB A:HIS210 3.5 40.3 1.0 CD2 A:HIS178 3.6 99.0 1.0 ND2 A:ASN253 4.0 30.7 1.0 OD2 A:ASP83 4.3 45.9 1.0 ND1 A:HIS84 4.3 55.5 1.0 CG A:HIS84 4.3 50.8 1.0 CD2 A:HIS210 4.4 59.5 1.0 ND1 A:HIS178 4.4 99.0 1.0 NE2 A:HIS210 4.5 55.6 1.0 CA A:HIS210 4.6 54.1 1.0 O A:HOH505 4.6 67.2 1.0 O A:HOH480 4.6 99.0 1.0 N A:GLY211 4.7 54.5 1.0 CG A:HIS178 4.7 99.0 1.0 C2 A:PGH325 4.8 53.8 1.0 OD1 A:ASP83 5.0 55.9 1.0

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


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 in Complex with Phosphoglycolohydroxamate within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn326 b:62.8 occ:1.00 NE2 B:HIS178 2.2 66.0 1.0 O1 B:PGH325 2.4 38.7 1.0 ND1 B:HIS210 2.5 35.4 1.0 NE2 B:HIS84 2.5 52.8 1.0 O2 B:PGH325 2.6 59.7 1.0 CE1 B:HIS178 2.8 64.2 1.0 C1 B:PGH325 3.0 51.8 1.0 CD2 B:HIS178 3.0 67.0 1.0 N2 B:PGH325 3.3 62.8 1.0 CE1 B:HIS84 3.3 32.0 1.0 CE1 B:HIS210 3.4 34.9 1.0 CG B:HIS210 3.5 23.0 1.0 CD2 B:HIS84 3.6 33.9 1.0 CB B:HIS210 3.7 18.8 1.0 ND1 B:HIS178 3.7 65.5 1.0 CG B:HIS178 3.8 72.7 1.0 O B:HOH380 4.0 57.4 1.0 O B:HOH455 4.2 54.1 1.0 N B:GLY211 4.4 28.4 1.0 CA B:HIS210 4.4 36.1 1.0 ND2 B:ASN253 4.4 30.7 1.0 ND1 B:HIS84 4.5 49.2 1.0 C2 B:PGH325 4.5 54.5 1.0 NE2 B:HIS210 4.5 32.0 1.0 CD2 B:HIS210 4.6 35.8 1.0 O1P B:PGH325 4.6 39.7 1.0 CG B:HIS84 4.7 42.7 1.0 OD1 B:ASP83 4.7 47.4 1.0 OD2 B:ASP83 4.7 36.6 1.0 C B:HIS210 4.9 31.0 1.0 O B:HOH474 5.0 48.4 1.0

A.Galkin, L.Kulakova, E.Melamud, L.Li, C.Wu, P.Mariano, D.Dunaway-Mariano, T.E.Nash, O.Herzberg. Characterization, Kinetics, and Crystal Structures of Fructose-1,6-Bisphosphate Aldolase From the Human Parasite, Giardia Lamblia. J.Biol.Chem. V. 282 4859 2007.
ISSN: ISSN 0021-9258
PubMed: 17166851
DOI: 10.1074/JBC.M609534200