Zinc in PDB 1e49: L-Fuculose 1-Phosphate Aldolase From Escherichia Coli Mutant N29L/S71A

All present enzymatic activity of L-Fuculose 1-Phosphate Aldolase From Escherichia Coli Mutant N29L/S71A:
4.1.2.17;

The structure of L-Fuculose 1-Phosphate Aldolase From Escherichia Coli Mutant N29L/S71A, PDB code: 1e49 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 / 2.53
Space group	P 4 21 2
Cell size a, b, c (Å), α, β, γ (°)	93.750, 93.750, 43.500, 90.00, 90.00, 90.00
R / Rfree (%)	14.2 / n/a

The binding sites of Zinc atom in the L-Fuculose 1-Phosphate Aldolase From Escherichia Coli Mutant N29L/S71A (pdb code 1e49). 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 N29L/S71A, PDB code: 1e49:

Zinc binding site 1 out of 1 in the L-Fuculose 1-Phosphate Aldolase From Escherichia Coli Mutant N29L/S71A


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 N29L/S71A within 5.0Å range: probe atom residue distance (Å) B Occ P:Zn303 b:17.5 occ:1.00 OE2 P:GLU73 2.0 24.3 1.0 NE2 P:HIS94 2.1 4.4 1.0 NE2 P:HIS92 2.1 9.4 1.0 NE2 P:HIS155 2.2 5.3 1.0 OE1 P:GLU73 2.3 22.4 1.0 CD P:GLU73 2.5 26.2 1.0 CD2 P:HIS155 3.0 6.0 1.0 CE1 P:HIS92 3.0 8.7 1.0 CD2 P:HIS94 3.0 6.0 1.0 CE1 P:HIS94 3.1 7.7 1.0 CD2 P:HIS92 3.2 9.4 1.0 CE1 P:HIS155 3.2 3.3 1.0 CG P:GLU73 4.0 27.4 1.0 ND1 P:HIS92 4.2 9.1 1.0 CG P:HIS155 4.2 7.4 1.0 CG P:HIS94 4.2 8.1 1.0 ND1 P:HIS94 4.2 8.0 1.0 ND1 P:HIS155 4.3 7.4 1.0 CG P:HIS92 4.3 9.2 1.0 O P:HOH405 4.3 35.3 1.0 CZ P:PHE76 4.7 17.5 1.0 CB P:GLU73 4.8 29.6 1.0 O P:ALA27 4.8 30.4 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