Zinc in PDB 1e4b: L-Fuculose 1-Phosphate Aldolase From Escherichia Coli Mutant N29Q

All present enzymatic activity of L-Fuculose 1-Phosphate Aldolase From Escherichia Coli Mutant N29Q:
4.1.2.17;

The structure of L-Fuculose 1-Phosphate Aldolase From Escherichia Coli Mutant N29Q, PDB code: 1e4b 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 / 1.84
Space group	P 4 21 2
Cell size a, b, c (Å), α, β, γ (°)	93.650, 93.650, 43.000, 90.00, 90.00, 90.00
R / Rfree (%)	16.5 / 20.4

The binding sites of Zinc atom in the L-Fuculose 1-Phosphate Aldolase From Escherichia Coli Mutant N29Q (pdb code 1e4b). 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 N29Q, PDB code: 1e4b:

Zinc binding site 1 out of 1 in the L-Fuculose 1-Phosphate Aldolase From Escherichia Coli Mutant N29Q


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 N29Q within 5.0Å range: probe atom residue distance (Å) B Occ P:Zn304 b:14.2 occ:1.00 OE2 P:GLU73 2.0 20.7 1.0 NE2 P:HIS94 2.0 11.5 1.0 NE2 P:HIS92 2.0 12.1 1.0 NE2 P:HIS155 2.1 10.6 1.0 CD P:GLU73 2.7 20.0 1.0 OE1 P:GLU73 2.7 20.3 1.0 CE1 P:HIS92 2.9 11.1 1.0 CD2 P:HIS94 2.9 11.3 1.0 CD2 P:HIS155 3.0 9.8 1.0 CE1 P:HIS94 3.1 12.6 1.0 CD2 P:HIS92 3.1 11.5 1.0 CE1 P:HIS155 3.2 11.3 1.0 O P:HOH2032 3.9 41.0 1.0 ND1 P:HIS92 4.1 11.2 1.0 CG P:HIS94 4.1 13.1 1.0 CG P:GLU73 4.2 18.9 1.0 CG P:HIS155 4.2 10.3 1.0 ND1 P:HIS94 4.2 12.2 1.0 CG P:HIS92 4.2 11.4 1.0 ND1 P:HIS155 4.2 10.7 1.0 CZ P:PHE76 4.5 16.2 1.0 O P:ALA27 4.6 35.9 1.0 NE2 P:GLN29 4.9 18.2 1.0 CB P:GLU73 5.0 19.5 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