Zinc in PDB 1e4c: L-Fuculose 1-Phosphate Aldolase From Escherichia Coli Mutant S71Q

All present enzymatic activity of L-Fuculose 1-Phosphate Aldolase From Escherichia Coli Mutant S71Q:
4.1.2.17;

The structure of L-Fuculose 1-Phosphate Aldolase From Escherichia Coli Mutant S71Q, PDB code: 1e4c was solved by A.C.Joerger, G.E.Schulz, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	10.00 / 1.66
Space group	P 4 21 2
Cell size a, b, c (Å), α, β, γ (°)	93.520, 93.520, 42.370, 90.00, 90.00, 90.00
R / Rfree (%)	16.4 / 20

The binding sites of Zinc atom in the L-Fuculose 1-Phosphate Aldolase From Escherichia Coli Mutant S71Q (pdb code 1e4c). 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 From Escherichia Coli Mutant S71Q, PDB code: 1e4c:

Zinc binding site 1 out of 1 in the L-Fuculose 1-Phosphate Aldolase From Escherichia Coli Mutant S71Q


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 From Escherichia Coli Mutant S71Q within 5.0Å range: probe atom residue distance (Å) B Occ P:Zn303 b:12.0 occ:1.00 NE2 P:HIS155 2.1 8.2 1.0 NE2 P:HIS92 2.1 8.2 1.0 NE2 P:HIS94 2.1 11.1 1.0 O P:HOH404 2.1 19.1 1.0 OE2 P:GLU73 2.2 15.4 1.0 CE1 P:HIS92 3.0 7.9 1.0 CD2 P:HIS155 3.1 9.1 1.0 CD2 P:HIS94 3.1 10.9 1.0 CD P:GLU73 3.1 15.6 1.0 CE1 P:HIS94 3.1 12.5 1.0 CE1 P:HIS155 3.1 10.2 1.0 CD2 P:HIS92 3.1 8.2 1.0 OE1 P:GLU73 3.3 16.6 1.0 O P:ALA27 4.1 18.5 1.0 ND1 P:HIS92 4.2 7.6 1.0 CG P:HIS155 4.2 8.7 1.0 ND1 P:HIS94 4.2 10.7 1.0 CG P:HIS94 4.2 9.9 1.0 ND1 P:HIS155 4.2 9.4 1.0 CG P:HIS92 4.2 8.5 1.0 CG P:GLU73 4.5 14.8 1.0 CZ P:PHE76 4.6 15.8 1.0

A.C.Joerger, C.Mueller-Dieckmann, G.E.Schulz. Structures of L-Fuculose-1-Phosphate Aldolase Mutants Outlining Motions During Catalysis J.Mol.Biol. V. 303 531 2000.
ISSN: ISSN 0022-2836
PubMed: 11054289
DOI: 10.1006/JMBI.2000.4153