Zinc in PDB 1zen: Class II Fructose-1,6-Bisphosphate Aldolase

All present enzymatic activity of Class II Fructose-1,6-Bisphosphate Aldolase:
4.1.2.13;

The structure of Class II Fructose-1,6-Bisphosphate Aldolase, PDB code: 1zen was solved by S.J.Cooper, G.A.Leonard, W.N.Hunter, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	6.00 / 2.50
Space group	P 61 2 2
Cell size a, b, c (Å), α, β, γ (°)	78.360, 78.360, 290.330, 90.00, 90.00, 120.00
R / Rfree (%)	24.3 / 32.6

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

Zinc binding site 1 out of 2 in the Class II Fructose-1,6-Bisphosphate Aldolase


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Class II Fructose-1,6-Bisphosphate Aldolase within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn359 b:34.6 occ:0.60 OD1 A:ASP109 2.5 19.5 1.0 OE2 A:GLU172 2.6 20.9 1.0 NE2 A:HIS264 2.6 33.2 1.0 NZ A:LYS284 2.8 33.5 1.0 OE1 A:GLU172 2.8 23.1 1.0 CD A:GLU172 3.0 23.7 1.0 CE1 A:HIS264 3.1 31.7 1.0 ND2 A:ASN286 3.2 26.3 1.0 NE2 A:HIS107 3.6 20.4 1.0 OD1 A:ASN286 3.6 17.2 1.0 CG A:ASP109 3.7 35.4 1.0 CD2 A:HIS264 3.8 39.6 1.0 CG A:ASN286 3.8 13.4 1.0 CE A:LYS284 3.8 30.1 1.0 CG1 A:VAL262 4.0 27.2 1.0 OE1 A:GLN59 4.1 19.9 1.0 SD A:MET142 4.2 33.0 1.0 ND1 A:HIS264 4.3 35.8 1.0 CD2 A:HIS107 4.4 20.2 1.0 CD A:LYS284 4.4 24.1 1.0 CE A:MET142 4.4 34.3 1.0 CE1 A:HIS107 4.5 15.3 1.0 CG A:GLU172 4.5 21.8 1.0 OD2 A:ASP109 4.6 27.6 1.0 CG A:MET142 4.6 24.1 1.0 CB A:ASP109 4.6 31.7 1.0 CG A:HIS264 4.7 31.8 1.0 CA A:ASP109 4.8 33.1 1.0 CB A:MET142 4.8 21.1 1.0

Zinc binding site 2 out of 2 in the Class II Fructose-1,6-Bisphosphate Aldolase


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Class II Fructose-1,6-Bisphosphate Aldolase within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn360 b:38.6 occ:1.00 ND1 A:HIS264 2.5 35.8 1.0 OE1 A:GLU174 2.5 36.2 1.0 NE2 A:HIS226 2.5 46.5 1.0 NE2 A:HIS110 2.7 34.7 1.0 OE2 A:GLU174 2.7 40.4 1.0 CD A:GLU174 2.9 25.9 1.0 CD2 A:HIS226 3.0 45.3 1.0 CE1 A:HIS110 3.1 32.3 1.0 CE1 A:HIS264 3.2 31.7 1.0 CG A:HIS264 3.5 31.8 1.0 CE1 A:HIS226 3.6 51.0 1.0 CB A:HIS264 3.8 35.2 1.0 CD2 A:HIS110 3.9 36.1 1.0 O A:HOH393 3.9 40.6 1.0 CE A:MET142 3.9 34.3 1.0 CG A:HIS226 4.2 52.0 1.0 CG A:GLU174 4.3 31.7 1.0 NE2 A:HIS264 4.4 33.2 1.0 ND1 A:HIS110 4.4 29.8 1.0 ND1 A:HIS226 4.5 50.1 1.0 CD2 A:HIS264 4.5 39.6 1.0 OD2 A:ASP144 4.6 45.4 1.0 CB A:ALA219 4.7 42.9 1.0 CG A:HIS110 4.8 30.3 1.0 O A:HOH376 4.8 29.0 1.0 CB A:GLU174 4.9 32.1 1.0

S.J.Cooper, G.A.Leonard, S.M.Mcsweeney, A.W.Thompson, J.H.Naismith, S.Qamar, A.Plater, A.Berry, W.N.Hunter. The Crystal Structure of A Class II Fructose-1,6-Bisphosphate Aldolase Shows A Novel Binuclear Metal-Binding Active Site Embedded in A Familiar Fold. Structure V. 4 1303 1996.
ISSN: ISSN 0969-2126
PubMed: 8939754
DOI: 10.1016/S0969-2126(96)00138-4