Zinc in PDB 1fua: L-Fuculose 1-Phosphate Aldolase Crystal Form T

All present enzymatic activity of L-Fuculose 1-Phosphate Aldolase Crystal Form T:
4.1.2.17;

The structure of L-Fuculose 1-Phosphate Aldolase Crystal Form T, PDB code: 1fua was solved by M.K.Dreyer, G.E.Schulz, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	10.00 / 1.92
Space group	P 4 21 2
Cell size a, b, c (Å), α, β, γ (°)	93.700, 93.700, 42.800, 90.00, 90.00, 90.00
R / Rfree (%)	18.6 / n/a

The binding sites of Zinc atom in the L-Fuculose 1-Phosphate Aldolase Crystal Form T (pdb code 1fua). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total only one binding site of Zinc was determined in the L-Fuculose 1-Phosphate Aldolase Crystal Form T, PDB code: 1fua:

Zinc binding site 1 out of 1 in the L-Fuculose 1-Phosphate Aldolase Crystal Form T


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of L-Fuculose 1-Phosphate Aldolase Crystal Form T within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn216 b:12.5 occ:1.00 OE2 A:GLU73 1.9 14.6 1.0 NE2 A:HIS155 2.0 6.5 1.0 NE2 A:HIS94 2.1 16.4 1.0 NE2 A:HIS92 2.1 7.5 1.0 OE1 A:GLU73 2.4 14.2 1.0 CD A:GLU73 2.5 12.9 1.0 CE1 A:HIS92 3.0 2.9 1.0 CD2 A:HIS155 3.0 7.4 1.0 CE1 A:HIS94 3.0 17.1 1.0 CE1 A:HIS155 3.0 7.0 1.0 CD2 A:HIS94 3.1 15.6 1.0 CD2 A:HIS92 3.2 6.0 1.0 CG A:GLU73 4.0 12.4 1.0 O A:HOH428 4.0 28.6 1.0 ND1 A:HIS155 4.2 7.3 1.0 ND1 A:HIS94 4.2 16.9 1.0 CG A:HIS155 4.2 5.5 1.0 ND1 A:HIS92 4.2 5.4 1.0 CG A:HIS94 4.2 16.6 1.0 CG A:HIS92 4.3 4.8 1.0 CZ A:PHE76 4.5 14.2 1.0 O A:ALA27 4.6 37.1 1.0 CE2 A:PHE76 4.8 12.6 1.0 CB A:GLU73 4.8 14.2 1.0

M.K.Dreyer, G.E.Schulz. Refined High-Resolution Structure of the Metal-Ion Dependent L-Fuculose-1-Phosphate Aldolase (Class II) From Escherichia Coli. Acta Crystallogr.,Sect.D V. 52 1082 1996.
ISSN: ISSN 0907-4449
PubMed: 15299567
DOI: 10.1107/S0907444996009146