Zinc in PDB 3fua: L-Fuculose-1-Phosphate Aldolase Crystal Form K

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

The structure of L-Fuculose-1-Phosphate Aldolase Crystal Form K, PDB code: 3fua 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 / 2.67
Space group	F 4 3 2
Cell size a, b, c (Å), α, β, γ (°)	183.000, 183.000, 183.000, 90.00, 90.00, 90.00
R / Rfree (%)	18.4 / 24.1

The structure of L-Fuculose-1-Phosphate Aldolase Crystal Form K also contains other interesting chemical elements:

Chlorine

(Cl)

1 atom

The binding sites of Zinc atom in the L-Fuculose-1-Phosphate Aldolase Crystal Form K (pdb code 3fua). 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 K, PDB code: 3fua:

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


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 K within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn216 b:11.6 occ:1.00 NE2 A:HIS155 2.0 2.3 1.0 NE2 A:HIS92 2.0 6.8 1.0 NE2 A:HIS94 2.0 9.6 1.0 OE2 A:GLU73 2.1 13.6 1.0 OE1 A:GLU73 2.5 14.7 1.0 CD A:GLU73 2.6 13.3 1.0 CE1 A:HIS94 2.7 8.6 1.0 CE1 A:HIS92 2.9 7.0 1.0 CE1 A:HIS155 2.9 2.1 1.0 CD2 A:HIS155 3.0 2.7 1.0 CD2 A:HIS92 3.1 6.4 1.0 CD2 A:HIS94 3.2 9.0 1.0 ND1 A:HIS94 3.9 8.9 1.0 ND1 A:HIS155 4.1 2.0 1.0 CG A:GLU73 4.1 11.2 1.0 ND1 A:HIS92 4.1 6.6 1.0 CG A:HIS94 4.1 6.8 1.0 CG A:HIS155 4.2 2.0 1.0 CG A:HIS92 4.2 5.3 1.0 CZ A:PHE76 4.4 4.2 1.0 O A:HOH457 4.9 36.3 1.0 CB A:GLU73 4.9 9.3 1.0 CE2 A:PHE76 5.0 4.3 1.0

M.K.Dreyer, G.E.Schulz. Catalytic Mechanism of the Metal-Dependent Fuculose Aldolase From Escherichia Coli As Derived From the Structure. J.Mol.Biol. V. 259 458 1996.
ISSN: ISSN 0022-2836
PubMed: 8676381
DOI: 10.1006/JMBI.1996.0332