Zinc in PDB 4fua: L-Fuculose-1-Phosphate Aldolase Complex with Pgh

All present enzymatic activity of L-Fuculose-1-Phosphate Aldolase Complex with Pgh:
4.1.2.17;

The structure of L-Fuculose-1-Phosphate Aldolase Complex with Pgh, PDB code: 4fua 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 / 2.43
Space group	F 4 3 2
Cell size a, b, c (Å), α, β, γ (°)	183.600, 183.600, 183.600, 90.00, 90.00, 90.00
R / Rfree (%)	18.5 / n/a

The binding sites of Zinc atom in the L-Fuculose-1-Phosphate Aldolase Complex with Pgh (pdb code 4fua). 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 Complex with Pgh, PDB code: 4fua:

Zinc binding site 1 out of 1 in the L-Fuculose-1-Phosphate Aldolase Complex with Pgh


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 Complex with Pgh within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn216 b:12.9 occ:1.00 O2 A:PGH217 1.9 16.4 1.0 NE2 A:HIS155 2.0 4.7 1.0 NE2 A:HIS94 2.0 2.0 1.0 NE2 A:HIS92 2.1 2.8 1.0 O1 A:PGH217 2.2 10.1 1.0 N2 A:PGH217 2.8 14.4 1.0 C1 A:PGH217 2.8 12.5 1.0 CE1 A:HIS155 2.9 7.1 1.0 CE1 A:HIS94 3.0 4.0 1.0 CD2 A:HIS94 3.1 3.5 1.0 CD2 A:HIS155 3.1 6.8 1.0 CD2 A:HIS92 3.1 2.9 1.0 CE1 A:HIS92 3.1 3.8 1.0 OE2 A:GLU73 4.0 2.9 1.0 ND1 A:HIS155 4.1 7.0 1.0 ND1 A:HIS94 4.1 4.8 1.0 CG A:HIS94 4.2 2.6 1.0 CG A:HIS155 4.2 6.2 1.0 ND1 A:HIS92 4.3 4.2 1.0 CG A:HIS92 4.3 3.5 1.0 C2 A:PGH217 4.3 11.2 1.0 N A:GLY28 4.6 15.9 1.0 CG A:GLU73 4.7 2.5 1.0 CD A:GLU73 4.7 5.4 1.0 ND2 A:ASN29 4.7 8.1 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